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Journal articles on the topic 'Serial crystallographie'

Author: Grafiati

Published: 31 May 2025

Last updated: 31 July 2025

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1

Nam, Ki-Hyun. "Approach of Serial Crystallography II." Crystals 11, no. 6 (2021): 655. http://dx.doi.org/10.3390/cryst11060655.

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Serial crystallography (SX) is an emerging X-ray crystallographic method for determining macromolecule structures. It can address concerns regarding the limitations of data collected by conventional crystallography techniques, which require cryogenic-temperature environments and allow crystals to accumulate radiation damage. Time-resolved SX studies using the pump-probe methodology provide useful information for understanding macromolecular mechanisms and structure fluctuation dynamics. This Special Issue deals with the serial crystallography approach using an X-ray free electron laser (XFEL)

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Nam, Ki. "Sample Delivery Media for Serial Crystallography." International Journal of Molecular Sciences 20, no. 5 (2019): 1094. http://dx.doi.org/10.3390/ijms20051094.

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X-ray crystallographic methods can be used to visualize macromolecules at high resolution. This provides an understanding of molecular mechanisms and an insight into drug development and rational engineering of enzymes used in the industry. Although conventional synchrotron-based X-ray crystallography remains a powerful tool for understanding molecular function, it has experimental limitations, including radiation damage, cryogenic temperature, and static structural information. Serial femtosecond crystallography (SFX) using X-ray free electron laser (XFEL) and serial millisecond crystallograp

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3

Gevorkov, Yaroslav, Anton Barty, Wolfgang Brehm, et al. "pinkIndexer – a universal indexer for pink-beam X-ray and electron diffraction snapshots." Acta Crystallographica Section A Foundations and Advances 76, no. 2 (2020): 121–31. http://dx.doi.org/10.1107/s2053273319015559.

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A crystallographic indexing algorithm, pinkIndexer, is presented for the analysis of snapshot diffraction patterns. It can be used in a variety of contexts including measurements made with a monochromatic radiation source, a polychromatic source or with radiation of very short wavelength. As such, the algorithm is particularly suited to automated data processing for two emerging measurement techniques for macromolecular structure determination: serial pink-beam X-ray crystallography and serial electron crystallography, which until now lacked reliable programs for analyzing many individual diff

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4

Wolff, Alexander M., Iris D. Young, Raymond G. Sierra, et al. "Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals." IUCrJ 7, no. 2 (2020): 306–23. http://dx.doi.org/10.1107/s205225252000072x.

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Innovative new crystallographic methods are facilitating structural studies from ever smaller crystals of biological macromolecules. In particular, serial X-ray crystallography and microcrystal electron diffraction (MicroED) have emerged as useful methods for obtaining structural information from crystals on the nanometre to micrometre scale. Despite the utility of these methods, their implementation can often be difficult, as they present many challenges that are not encountered in traditional macromolecular crystallography experiments. Here, XFEL serial crystallography experiments and MicroE

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Smith, Nathan, and Mark A. Wilson. "Understanding Cysteine Chemistry Using Conventional and Serial X-ray Protein Crystallography." Crystals 12, no. 11 (2022): 1671. http://dx.doi.org/10.3390/cryst12111671.

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Proteins that use cysteine residues for catalysis or regulation are widely distributed and intensively studied, with many biomedically important examples. Enzymes where cysteine is a catalytic nucleophile typically generate covalent catalytic intermediates whose structures are important for understanding mechanism and for designing targeted inhibitors. The formation of catalytic intermediates can change enzyme conformational dynamics, sometimes activating protein motions that are important for catalytic turnover. However, these transiently populated intermediate species have been challenging t

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Horrell, Sam, Svetlana V. Antonyuk, Robert R. Eady, S. Samar Hasnain, Michael A. Hough, and Richard W. Strange. "Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal." IUCrJ 3, no. 4 (2016): 271–81. http://dx.doi.org/10.1107/s205225251600823x.

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Relating individual protein crystal structures to an enzyme mechanism remains a major and challenging goal for structural biology. Serial crystallography using multiple crystals has recently been reported in both synchrotron-radiation and X-ray free-electron laser experiments. In this work, serial crystallography was used to obtain multiple structures serially from one crystal (MSOX) to studyin crystalloenzyme catalysis. Rapid, shutterless X-ray detector technology on a synchrotron MX beamline was exploited to perform low-dose serial crystallography on a single copper nitrite reductase crystal

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Yu, Li, Zhijun Wang, Qin Xu, et al. "An Electrospinning Sample Delivery Device for Synchrotron-Based Biomacromolecule Serial Crystallography Research." Quantum Beam Science 9, no. 2 (2025): 17. https://doi.org/10.3390/qubs9020017.

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Serial crystallography is a rapidly advancing experimental technology that has seen significant development in recent years. This technique enables the continuous delivery of a series of protein crystal samples to the X-ray beam, allowing for the collection of diffraction data from a large number of crystals at ambient temperature. Despite its advancements, serial crystallography still possesses considerable potential for further development within synchrotron radiation platforms. Currently, several challenges hinder the progress of this technology, including the preparation of numerous microc

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8

Mehrabi, P., R. Bücker, G. Bourenkov, et al. "Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison." Science Advances 7, no. 12 (2021): eabf1380. http://dx.doi.org/10.1126/sciadv.abf1380.

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For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective

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9

Coquelle, Nicolas, Aaron S. Brewster, Ulrike Kapp, et al. "Raster-scanning serial protein crystallography using micro- and nano-focused synchrotron beams." Acta Crystallographica Section D Biological Crystallography 71, no. 5 (2015): 1184–96. http://dx.doi.org/10.1107/s1399004715004514.

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High-resolution structural information was obtained from lysozyme microcrystals (20 µm in the largest dimension) using raster-scanning serial protein crystallography on micro- and nano-focused beamlines at the ESRF. Data were collected at room temperature (RT) from crystals sandwiched between two silicon nitride wafers, thereby preventing their drying, while limiting background scattering and sample consumption. In order to identify crystal hits, new multi-processing and GUI-driven Python-based pre-analysis software was developed, namedNanoPeakCell, that was able to read data from a variety of

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10

Ren, Zhong, Cong Wang, Heewhan Shin, et al. "An automated platform for in situ serial crystallography at room temperature." IUCrJ 7, no. 6 (2020): 1009–18. http://dx.doi.org/10.1107/s2052252520011288.

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Direct observation of functional motions in protein structures is highly desirable for understanding how these nanomachineries of life operate at the molecular level. Because cryogenic temperatures are non-physiological and may prohibit or even alter protein structural dynamics, it is necessary to develop robust X-ray diffraction methods that enable routine data collection at room temperature. We recently reported a crystal-on-crystal device to facilitate in situ diffraction of protein crystals at room temperature devoid of any sample manipulation. Here an automated serial crystallography plat

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11

Spence, John C. H. "Serial Crystallography: Preface." Crystals 10, no. 2 (2020): 135. http://dx.doi.org/10.3390/cryst10020135.

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The history of serial crystallography (SC) has its origins in the earliest attempts to merge data from several crystals. This preface provides an overview of some recent work, with a survey of the rapid advances made over the past decade in both sample delivery and data analysis.

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Martin-Garcia, Jose M., and Shibom Basu. "Macromolecular Serial Crystallography." Crystals 10, no. 12 (2020): 1079. http://dx.doi.org/10.3390/cryst10121079.

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Within the structural biology field, X-ray crystallography prevails as the dominant technique to determine the structures of macromolecules, producing, as of November 2020, more than 150,000 structures since its inception (https://www [...]

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13

Chapman, Henry N. "Serial Femtosecond Crystallography." Synchrotron Radiation News 28, no. 6 (2015): 20–24. http://dx.doi.org/10.1080/08940886.2015.1101323.

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14

Heymann, Michael, Achini Opthalage, Jennifer L. Wierman, et al. "Room-temperature serial crystallography using a kinetically optimized microfluidic device for protein crystallization and on-chip X-ray diffraction." IUCrJ 1, no. 5 (2014): 349–60. http://dx.doi.org/10.1107/s2052252514016960.

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An emulsion-based serial crystallographic technology has been developed, in which nanolitre-sized droplets of protein solution are encapsulated in oil and stabilized by surfactant. Once the first crystal in a drop is nucleated, the small volume generates a negative feedback mechanism that lowers the supersaturation. This mechanism is exploited to produce one crystal per drop. Diffraction data are measured, one crystal at a time, from a series of room-temperature crystals stored on an X-ray semi-transparent microfluidic chip, and a 93% complete data set is obtained by merging single diffraction

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15

Kim, Yongsam, and Ki Hyun Nam. "Pink-Beam Serial Synchrotron Crystallography at Pohang Light Source II." Crystals 12, no. 11 (2022): 1637. http://dx.doi.org/10.3390/cryst12111637.

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Serial crystallography (SX) enables the determination of room-temperature structures with minimal radiation damage. The photon flux of the pink beam of 1.2% bandwidth (BW) is one order higher than that of the monochromatic beam from a silicon crystal monochromator, and the energy resolution of 1.2% BW is enough to solve the structure; therefore, it is useful to use the pink beam for time-resolved serial synchrotron crystallography (SSX). Here, we demonstrate a pink-beam serial synchrotron crystallographic study at the 1C beamline at the Pohang Light Source II. Lysozyme crystals embedded in a b

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16

Hadian-Jazi, Marjan, Marc Messerschmidt, Connie Darmanin, Klaus Giewekemeyer, Adrian P. Mancuso, and Brian Abbey. "A peak-finding algorithm based on robust statistical analysis in serial crystallography." Journal of Applied Crystallography 50, no. 6 (2017): 1705–15. http://dx.doi.org/10.1107/s1600576717014340.

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The recent development of serial crystallography at synchrotron and X-ray free-electron laser (XFEL) sources is producing crystallographic datasets of ever increasing volume. The size of these datasets is such that fast and efficient analysis presents a range of challenges that have to be overcome to enable real-time data analysis, which is essential for the effective management of XFEL experiments. Among the blocks which constitute the analysis pipeline, one major bottleneck is `peak finding', whose goal is to identify the Bragg peaks within (often) noisy diffraction patterns. Development of

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17

Dworkowski, Florian, Ezequiel Panepucci, Claude Pradervand, et al. "Recent developments at the MX beamline X10SA at the SLS." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1731. http://dx.doi.org/10.1107/s2053273314082680.

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The three macromolecular crystallography (MX) beamlines at the Swiss Light Source (SLS) rank among the most productive in Europe. The very successful design of the first beamline, X06SA, inaugurated in 2001, was the basis for the second beamline, X10SA, operated by the Paul Scherrer Institut and financed by the partners Max Planck Society, Novartis and Hofmann-La Roche. To keep up with the increasing demand for high throughput crystallographic experiments, especially in an industrial environment, as well as the rising interest in more challenging targets, the beamline is under constant develop

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18

Waltersperger, Sandro, Vincent Olieric, Claude Pradervand, et al. "PRIGo: a new multi-axis goniometer for macromolecular crystallography." Journal of Synchrotron Radiation 22, no. 4 (2015): 895–900. http://dx.doi.org/10.1107/s1600577515005354.

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The Parallel Robotics Inspired Goniometer (PRIGo) is a novel compact and high-precision goniometer providing an alternative to (mini-)kappa, traditional three-circle goniometers and Eulerian cradles used for sample reorientation in macromolecular crystallography. Based on a combination of serial and parallel kinematics, PRIGo emulates an arc. It is mounted on an air-bearing stage for rotation around ω and consists of four linear positioners working synchronously to achievex, y, ztranslations and χ rotation (0–90°), followed by a φ stage (0–360°) for rotation around the sample holder axis. Owin

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19

Nam, Ki Hyun. "Serial X-ray Crystallography." Crystals 12, no. 1 (2022): 99. http://dx.doi.org/10.3390/cryst12010099.

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Serial crystallography (SX) is an emerging technique to determine macromolecules at room temperature. SX with a pump–probe experiment provides the time-resolved dynamics of target molecules. SX has developed rapidly over the past decade as a technique that not only provides room-temperature structures with biomolecules, but also has the ability to time-resolve their molecular dynamics. The serial femtosecond crystallography (SFX) technique using an X-ray free electron laser (XFEL) has now been extended to serial synchrotron crystallography (SSX) using synchrotron X-rays. The development of a v

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20

Nam, Ki Hyun. "Approach of Serial Crystallography." Crystals 10, no. 10 (2020): 854. http://dx.doi.org/10.3390/cryst10100854.

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Radiation damage and cryogenic sample environment are an experimental limitation observed in the traditional X-ray crystallography technique. However, the serial crystallography (SX) technique not only helps to determine structures at room temperature with minimal radiation damage, but it is also a useful tool for profound understanding of macromolecules. Moreover, it is a new tool for time-resolved studies. Over the past 10 years, various sample delivery techniques and data collection strategies have been developed in the SX field. It also has a wide range of applications in instruments rangi

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21

Gorel, Alexander, Ilme Schlichting, and Thomas R. M. Barends. "Discerning best practices in XFEL-based biological crystallography – standards for nonstandard experiments." IUCrJ 8, no. 4 (2021): 532–43. http://dx.doi.org/10.1107/s205225252100467x.

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Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) is a novel tool in structural biology. In contrast to conventional crystallography, SFX relies on merging partial intensities acquired with X-ray beams of often randomly fluctuating properties from a very large number of still diffraction images of generally randomly oriented microcrystals. For this reason, and possibly due to limitations of the still evolving data-analysis programs, XFEL-derived SFX data are typically of a lower quality than `standard' crystallographic data. In contrast with this, the studies perfo

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22

White, Thomas A., Anton Barty, Francesco Stellato, et al. "Crystallographic data processing for free-electron laser sources." Acta Crystallographica Section D Biological Crystallography 69, no. 7 (2013): 1231–40. http://dx.doi.org/10.1107/s0907444913013620.

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A processing pipeline for diffraction data acquired using the `serial crystallography' methodology with a free-electron laser source is described with reference to the crystallographic analysis suiteCrystFELand the pre-processing programCheetah. A detailed analysis of the nature and impact of indexing ambiguities is presented. Simulations of the Monte Carlo integration scheme, which accounts for the partially recorded nature of the diffraction intensities, are presented and show that the integration of partial reflections could be made to converge more quickly if the bandwidth of the X-rays we

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23

Assmann, Greta, Wolfgang Brehm, and Kay Diederichs. "Identification of rogue datasets in serial crystallography." Journal of Applied Crystallography 49, no. 3 (2016): 1021–28. http://dx.doi.org/10.1107/s1600576716005471.

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Advances in beamline optics, detectors and X-ray sources allow new techniques of crystallographic data collection. In serial crystallography, a large number of partial datasets from crystals of small volume are measured. Merging of datasets from different crystals in order to enhance data completeness and accuracy is only valid if the crystals are isomorphous,i.e.sufficiently similar in cell parameters, unit-cell contents and molecular structure. Identification and exclusion of non-isomorphous datasets is therefore indispensable and must be done by means of suitable indicators. To identify rog

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Adams, Patrick, Jack Binns, Tamar L. Greaves, and Andrew V. Martin. "The Sensitivity of the Pair-Angle Distribution Function to Protein Structure." Crystals 10, no. 9 (2020): 724. http://dx.doi.org/10.3390/cryst10090724.

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The continued development of X-ray free-electron lasers and serial crystallography techniques has opened up new experimental frontiers. Nanoscale dynamical processes such as crystal growth can now be probed at unprecedented time and spatial resolutions. Pair-angle distribution function (PADF) analysis is a correlation-based technique that has the potential to extend the limits of current serial crystallography experiments, by relaxing the requirements for crystal order, size and number density per exposure. However, unlike traditional crystallographic methods, the PADF technique does not recov

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Vlahakis, Niko, James Holton, Nicholas K. Sauter, Peter Ercius, Aaron S. Brewster, and Jose A. Rodriguez. "3D Nanocrystallography and the Imperfect Molecular Lattice." Annual Review of Physical Chemistry 75, no. 1 (2024): 483–508. http://dx.doi.org/10.1146/annurev-physchem-083122-105226.

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Crystallographic analysis relies on the scattering of quanta from arrays of atoms that populate a repeating lattice. While large crystals built of lattices that appear ideal are sought after by crystallographers, imperfections are the norm for molecular crystals. Additionally, advanced X-ray and electron diffraction techniques, used for crystallography, have opened the possibility of interrogating micro- and nanoscale crystals, with edges only millions or even thousands of molecules long. These crystals exist in a size regime that approximates the lower bounds for traditional models of crystal

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Martin-Garcia, Jose M. "Macromolecular Serial Crystallography (Volume II)." Crystals 12, no. 6 (2022): 768. http://dx.doi.org/10.3390/cryst12060768.

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The successful adaptation of the serial macromolecular crystallography approach at most 3rd generation synchrotron facilities allows a fruitful synergy between synchrotrons and XFELs that have accelerated the access and impact of this approach to an even larger community [...]

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27

Meents, Alke, Sebastian Günther, Patrick Reinke, Vincent Hennicke, and Pontus Fischer. "Low-background serial crystallography experiments." Acta Crystallographica Section A Foundations and Advances 77, a1 (2021): a248. http://dx.doi.org/10.1107/s0108767321097518.

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28

Weierstall, U. J., J. C. H. Spence, D. Starodub, et al. "Diffractive imaging and serial crystallography." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C129. http://dx.doi.org/10.1107/s0108767308095834.

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29

Spence, J. C. "Serial crystallography using protein beams." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C114. http://dx.doi.org/10.1107/s0108767308096359.

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30

Rossmann, Michael G. "Serial crystallography using synchrotron radiation." IUCrJ 1, no. 2 (2014): 84–86. http://dx.doi.org/10.1107/s2052252514000499.

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31

Wright, Jonathan P. "Serial crystallography for the masses?" IUCrJ 2, no. 1 (2015): 3–4. http://dx.doi.org/10.1107/s2052252514026803.

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32

Rabe, Patrick, John H. Beale, Agata Butryn, et al. "Anaerobic fixed-target serial crystallography." IUCrJ 7, no. 5 (2020): 901–12. http://dx.doi.org/10.1107/s2052252520010374.

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Cryogenic X-ray diffraction is a powerful tool for crystallographic studies on enzymes including oxygenases and oxidases. Amongst the benefits that cryo-conditions (usually employing a nitrogen cryo-stream at 100 K) enable, is data collection of dioxygen-sensitive samples. Although not strictly anaerobic, at low temperatures the vitreous ice conditions severely restrict O2 diffusion into and/or through the protein crystal. Cryo-conditions limit chemical reactivity, including reactions that require significant conformational changes. By contrast, data collection at room temperature imposes fewe

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Ayyer, Kartik, Oleksandr M. Yefanov, Dominik Oberthuer, et al. "Improving resolution in serial crystallography." Acta Crystallographica Section A Foundations and Advances 71, a1 (2015): s16. http://dx.doi.org/10.1107/s2053273315099738.

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Sierra, Raymond G., Hartawan Laksmono, Jan Kern, et al. "Nanoflow electrospinning serial femtosecond crystallography." Acta Crystallographica Section D Biological Crystallography 68, no. 11 (2012): 1584–87. http://dx.doi.org/10.1107/s0907444912038152.

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An electrospun liquid microjet has been developed that delivers protein microcrystal suspensions at flow rates of 0.14–3.1 µl min−1to perform serial femtosecond crystallography (SFX) studies with X-ray lasers. Thermolysin microcrystals flowed at 0.17 µl min−1and diffracted to beyond 4 Å resolution, producing 14 000 indexable diffraction patterns, or four per second, from 140 µg of protein. Nanoflow electrospinning extends SFX to biological samples that necessitate minimal sample consumption.

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HASEGAWA, Kazuya, and Takashi KUMASAKA. "Room Temperature Serial Synchrotron Crystallography." Nihon Kessho Gakkaishi 64, no. 4 (2022): 294–99. http://dx.doi.org/10.5940/jcrsj.64.294.

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Nam, Ki Hyun. "Serial X-ray Crystallography II." Crystals 13, no. 2 (2023): 222. http://dx.doi.org/10.3390/cryst13020222.

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Traditional macromolecular crystallography (MX) and recently spotlighted cryogenic electron microscopy (Cryo-EM) techniques have contributed greatly to the development of macromolecule structures and the related fields [...]

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Nam, Ki Hyun. "Guide to serial synchrotron crystallography." Current Research in Structural Biology 7 (2024): 100131. http://dx.doi.org/10.1016/j.crstbi.2024.100131.

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Hutchison, Christopher D. M., and Jasper J. van Thor. "Optical control, selection and analysis of population dynamics in ultrafast protein X-ray crystallography." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 377, no. 2145 (2019): 20170474. http://dx.doi.org/10.1098/rsta.2017.0474.

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Ultrafast pump-probe X-ray crystallography has now been established at X-ray free electron lasers that operate at hard X-ray energies. We discuss the performance and development of current applications in terms of the available data quality and sensitivity to detect and analyse structural dynamics. A discussion of technical capabilities expected at future high repetition rate applications as well as future non-collinear multi-pulse schemes focuses on the possibility to advance the technique to the practical application of the X-ray crystallographic equivalent of an impulse time-domain Raman me

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Muench, Stephen P., Svetlana V. Antonyuk, and S. Samar Hasnain. "The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryoEM." IUCrJ 6, no. 2 (2019): 167–77. http://dx.doi.org/10.1107/s2052252519002422.

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Structural biology continues to benefit from an expanding toolkit, which is helping to gain unprecedented insight into the assembly and organization of multi-protein machineries, enzyme mechanisms and ligand/inhibitor binding. The combination of results from X-ray free-electron lasers (XFELs), modern synchrotron crystallographic beamlines and cryo-electron microscopy (cryoEM) is proving to be particularly powerful. The highly brilliant undulator beamlines at modern synchrotron facilities have empowered the crystallographic revolution of high-throughput structure determination at high resolutio

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Sharma, Amit, Linda Johansson, Elin Dunevall, Weixiao Y. Wahlgren, Richard Neutze, and Gergely Katona. "Asymmetry in serial femtosecond crystallography data." Acta Crystallographica Section A Foundations and Advances 73, no. 2 (2017): 93–101. http://dx.doi.org/10.1107/s2053273316018696.

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Serial crystallography is an increasingly important approach to protein crystallography that exploits both X-ray free-electron laser (XFEL) and synchrotron radiation. Serial crystallography recovers complete X-ray diffraction data by processing and merging diffraction images from thousands of randomly oriented non-uniform microcrystals, of which all observations are partial Bragg reflections. Random fluctuations in the XFEL pulse energy spectrum, variations in the size and shape of microcrystals, integrating over millions of weak partial observations and instabilities in the XFEL beam position

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Doppler, Diandra, Mohammad T. Rabbani, Romain Letrun, et al. "Co-flow injection for serial crystallography at X-ray free-electron lasers." Journal of Applied Crystallography 55, no. 1 (2022): 1–13. http://dx.doi.org/10.1107/s1600576721011079.

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Serial femtosecond crystallography (SFX) is a powerful technique that exploits X-ray free-electron lasers to determine the structure of macromolecules at room temperature. Despite the impressive exposition of structural details with this novel crystallographic approach, the methods currently available to introduce crystals into the path of the X-ray beam sometimes exhibit serious drawbacks. Samples requiring liquid injection of crystal slurries consume large quantities of crystals (at times up to a gram of protein per data set), may not be compatible with vacuum configurations on beamlines or

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Beale, John H., Rachel Bolton, Stephen A. Marshall, et al. "Successful sample preparation for serial crystallography experiments." Journal of Applied Crystallography 52, no. 6 (2019): 1385–96. http://dx.doi.org/10.1107/s1600576719013517.

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Serial crystallography, at both synchrotron and X-ray free-electron laser light sources, is becoming increasingly popular. However, the tools in the majority of crystallization laboratories are focused on producing large single crystals by vapour diffusion that fit the cryo-cooled paradigm of modern synchrotron crystallography. This paper presents several case studies and some ideas and strategies on how to perform the conversion from a single crystal grown by vapour diffusion to the many thousands of micro-crystals required for modern serial crystallography grown by batch crystallization. The

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Nanao, Max, Shibom Basu, Ulrich Zander, et al. "ID23-2: an automated and high-performance microfocus beamline for macromolecular crystallography at the ESRF." Journal of Synchrotron Radiation 29, no. 2 (2022): 581–90. http://dx.doi.org/10.1107/s1600577522000984.

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ID23-2 is a fixed-energy (14.2 keV) microfocus beamline at the European Synchrotron Radiation Facility (ESRF) dedicated to macromolecular crystallography. The optics and sample environment have recently been redesigned and rebuilt to take full advantage of the upgrade of the ESRF to the fourth generation Extremely Brilliant Source (ESRF-EBS). The upgraded beamline now makes use of two sets of compound refractive lenses and multilayer mirrors to obtain a highly intense (>1013 photons s−1) focused microbeam (minimum size 1.5 µm × 3 µm full width at half-maximum). The sample environment now in

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Dejoie, Catherine, and Nobumichi Tamura. "Pattern-matching indexing of Laue and monochromatic serial crystallography data for applications in materials science." Journal of Applied Crystallography 53, no. 3 (2020): 824–36. http://dx.doi.org/10.1107/s160057672000521x.

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Serial crystallography data can be challenging to index, as each frame is processed individually, rather than being processed as a whole like in conventional X-ray single-crystal crystallography. An algorithm has been developed to index still diffraction patterns arising from small-unit-cell samples. The algorithm is based on the matching of reciprocal-lattice vector pairs, as developed for Laue microdiffraction data indexing, combined with three-dimensional pattern matching using a nearest-neighbors approach. As a result, large-bandpass data (e.g. 5–24 keV energy range) and monochromatic data

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Schneider, Dieter K., Wuxian Shi, Babak Andi, et al. "FMX – the Frontier Microfocusing Macromolecular Crystallography Beamline at the National Synchrotron Light Source II." Journal of Synchrotron Radiation 28, no. 2 (2021): 650–65. http://dx.doi.org/10.1107/s1600577520016173.

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Two new macromolecular crystallography (MX) beamlines at the National Synchrotron Light Source II, FMX and AMX, opened for general user operation in February 2017 [Schneider et al. (2013). J. Phys. Conf. Ser. 425, 012003; Fuchs et al. (2014). J. Phys. Conf. Ser. 493, 012021; Fuchs et al. (2016). AIP Conf. Proc. SRI2015, 1741, 030006]. FMX, the micro-focusing Frontier MX beamline in sector 17-ID-2 at NSLS-II, covers a 5–30 keV photon energy range and delivers a flux of 4.0 × 1012 photons s−1 at 1 Å into a 1 µm × 1.5 µm to 10 µm × 10 µm (V × H) variable focus, expected to reach 5 × 1012 photons

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Dilanian, Ruben A., Sophie R. Williams, Andrew V. Martin, Victor A. Streltsov, and Harry M. Quiney. "Whole-pattern fitting technique in serial femtosecond nanocrystallography." IUCrJ 3, no. 2 (2016): 127–38. http://dx.doi.org/10.1107/s2052252516001238.

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Serial femtosecond X-ray crystallography (SFX) has created new opportunities in the field of structural analysis of protein nanocrystals. The intensity and timescale characteristics of the X-ray free-electron laser sources used in SFX experiments necessitate the analysis of a large collection of individual crystals of variable shape and quality to ultimately solve a single, average crystal structure. Ensembles of crystals are commonly encountered in powder diffraction, but serial crystallography is different because each crystal is measured individually and can be orientedviaindexing and merge

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De Zitter, Elke, Martin Savko, Damien Jeangerard, et al. "Serial-MOF: developing serial crystallography methods for MOF nano-crystals." Acta Crystallographica Section A Foundations and Advances 75, a2 (2019): e527-e527. http://dx.doi.org/10.1107/s2053273319090296.

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Marin, Egor, Daniil Vakhrameev, Anastasiia Gusach, et al. "Abstract P-4: Robust Method for Background Subtraction in Serial X-ray Diffraction Data." International Journal of Biomedicine 11, Suppl_1 (2021): S12. http://dx.doi.org/10.21103/ijbm.11.suppl_1.p4.

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Background: Membrane receptors play an important role in signal transduction across the cell membrane in all living organisms. Their structural studies have been enabled by multiple technological breakthroughs in their heterologous expression, stabilization, crystallization, and crystallographic data collection as well as in cryogenic electron microscopy (cryoEM). During the last decade, serial femtosecond crystallography (SFX) using X-ray free electron lasers (XFELs) has enabled structure determination of previously inaccessible proteins, including several G-protein-coupled receptors (GPCR),

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Mittan-Moreau, David, Daniel Paley, Nicholas Sauter, and Aaron Brewster. "Robust error calibration for serial crystallography." Structural Dynamics 12, no. 2_Supplement (2025): A362. https://doi.org/10.1063/4.0000668.

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In macromolecular crystallography (MX), integrated intensities’ final uncertainties are typically calculated by an empirical transformation of initial counting statistics uncertainties, a procedure generally known as error calibration. Existing MX error calibration algorithms were designed for single-crystal rotational diffraction experiments. This work describes their further adaptation to serial femtosecond crystallography and is motivated by fundamental differences in data and experimentation between these methods. We propose a new parameterized error transformation that applies different l

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Hogan-Lamarre, Pascal. "Recent advances in serial electron crystallography." Acta Crystallographica Section A Foundations and Advances 76, a1 (2020): a88. http://dx.doi.org/10.1107/s0108767320099110.

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