Results 71 to 80 of about 4,136 (214)

Serial femtosecond crystallography opens new avenues for Structural Biology [PDF]

Protein & Peptide Letters, 2016
Free electron lasers (FELs) provide X-ray pulses in the femtosecond time domain with up to 10(12) higher photon flux than synchrotrons and open new avenues for the determination of difficult to crystallize proteins, like large complexes and human membrane proteins.
Jesse, Coe, Petra, Fromme
openaire   +2 more sources

Multi‐Crystal X‐Ray Diffraction (MCXRD) Bridges the Crystallographic Characterisation Gap in Chemistry and Materials Science: Application to MOFs

Angewandte Chemie, EarlyView.
Multi‐crystal X‐ray diffraction (MCXRD) methods allow accurate structural characterisation with crystals too small for single‐crystal X‐ray diffraction and too large for electron diffraction, as demonstrated here for metal‐organic frameworks, and alleviate the radiation‐induced chemical changes that can result from using high‐intensity X‐ray sources to
Joshua P. Smith, Rebecca Smith, Thomas M. Roseveare, Dominic Bara, Alexander J. R. Thom, Ross S. Forgan, Mark R. Warren, Anna J. Warren, Robin L. Owen, Lee Brammer   +9 more
wiley   +2 more sources

The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryoEM

IUCrJ, 2019
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.
Stephen P. Muench, Svetlana V. Antonyuk, S. Samar Hasnain   +2 more
doaj   +1 more source

Native sulfur/chlorine SAD phasing for serial femtosecond crystallography [PDF]

Acta Crystallographica Section D Biological Crystallography, 2015
Serial femtosecond crystallography (SFX) allows structures to be determined with minimal radiation damage. However, phasing native crystals in SFX is not very common. Here, the structure determination of native lysozyme from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of sulfur and chlorine at a wavelength of 1.77 Å ...
Nakane, T, Song, CY, Suzuki, M, Nango, E, Kobayashi, J, Masuda, T, Inoue, S, Mizohata, E, Nakatsu, T, Tanaka, T, Tanaka, R, Shimamura, T, Tono, K, Joti, Y, Kameshima, T, Hatsui, T, Yabashi, M, Nureki, O, Iwata, S, Sugahara, M   +19 more
openaire   +3 more sources

An outlook on using serial femtosecond crystallography in drug discovery. [PDF]

Expert Opin Drug Discov, 2019
Introduction: X-ray crystallography has made important contributions to modern drug development but its application to many important drug targets has been extremely challenging. The recent emergence of X-ray free electron lasers (XFELs) and advancements in serial femtosecond crystallography (SFX) have offered new opportunities to overcome limitations ...
Mishin A, Gusach A, Luginina A, Marin E, Borshchevskiy V, Cherezov V.   +5 more
europepmc   +4 more sources

Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography

Structural Dynamics, 2015
We present a crystallography chip enabling in situ room temperature crystallography at microfocus synchrotron beamlines and X-ray free-electron laser (X-FEL) sources.
C. Mueller, A. Marx, S. W. Epp, Y. Zhong, A. Kuo, A. R. Balo, J. Soman, F. Schotte, H. T. Lemke, R. L. Owen, E. F. Pai, A. R. Pearson, J. S. Olson, P. A. Anfinrud, O. P. Ernst, R. J. Dwayne Miller   +15 more
doaj   +1 more source

Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy

Nature Communications, 2020
rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resolved ...
Joyce Woodhouse, Gabriela Nass Kovacs, Nicolas Coquelle, Lucas M. Uriarte, Virgile Adam, Thomas R. M. Barends, Martin Byrdin, Eugenio de la Mora, R. Bruce Doak, Mikolaj Feliks, Martin Field, Franck Fieschi, Virginia Guillon, Stefan Jakobs, Yasumasa Joti, Pauline Macheboeuf, Koji Motomura, Karol Nass, Shigeki Owada, Christopher M. Roome, Cyril Ruckebusch, Giorgio Schirò, Robert L. Shoeman, Michel Thepaut, Tadashi Togashi, Kensuke Tono, Makina Yabashi, Marco Cammarata, Lutz Foucar, Dominique Bourgeois, Michel Sliwa, Jacques-Philippe Colletier, Ilme Schlichting, Martin Weik   +33 more
doaj   +1 more source

Data processing pipeline for serial femtosecond crystallography at SACLA [PDF]

Journal of Applied Crystallography, 2016
A data processing pipeline for serial femtosecond crystallography at SACLA was developed, based onCheetah[Bartyet al.(2014).J. Appl. Cryst.47, 1118–1131] andCrystFEL[Whiteet al.(2016).J. Appl. Cryst.49, 680–689]. The original programs were adapted for data acquisition through the SACLA API, thread and inter-node parallelization, and efficient image ...
Nakane, Takanori, Joti, Yasumasa, Tono, Kensuke, Yabashi, Makina, Nango, Eriko, Iwata, So, Ishitani, Ryuichiro, Nureki, Osamu   +7 more
openaire   +2 more sources

Liquid sample delivery techniques for serial femtosecond crystallography [PDF]

Philosophical Transactions of the Royal Society B: Biological Sciences, 2014
X-ray free-electron lasers overcome the problem of radiation damage in protein crystallography and allow structure determination from micro- and nanocrystals at room temperature. To ensure that consecutive X-ray pulses do not probe previously exposed crystals, the sample needs to be replaced with the X-ray repetition rate, which ranges from 120 Hz at ...
openaire   +2 more sources

Atomic resolution structure of serine protease proteinase K at ambient temperature [PDF]

, 2017
Atomic resolution structures (beyond 1.20 ?) at ambient temperature, which is usually hampered by the radiation damage in synchrotron X-ray crystallography (SRX), will add to our understanding of the structure-function relationships of enzymes.
Hatsui, T., Inoue, S., Iwata, S., Joti, Y., Kameshima, T., Masuda, T., Mikami, B., Nakane, T., Nango, E., Numata, K., Nureki, O., Song, C., Sugahara, M., Suzuki, M., Tanaka, R., Tono, K., Yabashi, M.   +16 more
core   +1 more source