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De novo protein crystal structure determination from X-ray free-electron laser data
08 Jan 2014 | Publications | Contributor(s): K. Nass, S. Botha, G. J. Williams, J. E. Koglin, T. R. Barends, R. L. Shoeman, L. Foucar, I. Schlichting, S. Boutet, R. B. Doak, Mark Messerschmidt
The determination of protein crystal structures is hampered by the need for macroscopic crystals. X-ray free-electron lasers (FELs) provide extremely intense pulses of femtosecond duration, which …
https://www.bioxfel.org/resources/De-novo-protein-crystal-structure
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Protein structural ensembles are revealed by redefining X-ray electron density noise
06 Jan 2014 | Publications | Contributor(s): P. T. Lang, T. Alber, J. S. Fraser, James Holton
To increase the power of X-ray crystallography to determine not only the structures but also the motions of biomolecules, we developed methods to address two classic crystallographic problems: …
https://www.bioxfel.org/resources/Protein-structural-ensembles-are-revealed
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Crystallography: Sources of inspiration
31 Dec 2012 | Publications | Contributor(s): S. McSweeney, Petra Fromme
2014.
https://www.bioxfel.org/resources/Crystallography:-Sources-of-inspiration
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Lawrence Bragg, microdiffraction and X-ray lasers
31 Dec 2012 | Publications | Contributor(s): John Spence
https://www.bioxfel.org/resources/Lawrence-Bragg,-microdiffraction-and-X-ray
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Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state
03 May 2012 | Publications | Contributor(s): G. Haran, T. R. Sosnick, K. Plaxco, S. P. Meisburger, J. Hinshaw, T. Y. Yoo, Lois Pollack
The results of more than a dozen single-molecule Forster resonance energy transfer (smFRET) experiments suggest that chemically unfolded polypeptides invariably collapse from an expanded random coil …
https://www.bioxfel.org/resources/Small-angle-X-ray-scattering-and-single-molecule
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In vivo protein crystallization opens new routes in structural biology
29 Feb 2012 | Publications | Contributor(s): J. Andreasson, M. J. Bogan, K. Nass, H. Fleckenstein, X. Wang, D. P. Deponte, S. Boutet, B. Erk, L. Struder, J. Ullrich, H. Soltau, T. Ekeberg, C. Caleman, R. Koopmann, A. Hartmann, N. Kimmel, G. Hauser, J. Davidsson, M. M. Seibert, L. Gumprecht, R. B. Doak, D. Rolles, S. Stern, C. B. Wunderer, M. Duszenko, K. Cupelli, I. Schlichting, C. Y. Hampton, S. Bajt, A. V. Martin, P. Holl, G. Weidenspointner, L. Redecke, J. Schulz, H. Hirsemann, C. Bostedt, R. Hartmann, A. Barty, N. Coppola, F. Stellato, T. A. White, J. D. Bozek, M. Liang, L. Foucar, R. A. Kirian, H. Graafsma, D. Rehders, S. Kassemeyer, B. Rudek, M. Barthelmess, T. Stehle, C. Reich, R. L. Shoeman, A. Rudenko, N. Timneanu, G. J. Williams, J. Hajdu, L. Lomb, R. G. Sierra, A. Aquila, F. R. Maia, S. W. Epp, C. Betzel, Henry Chapman, Petra Fromme, Mark S. Hunter, Mark Messerschmidt, John Spence, Uwe Weierstall
Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis.
https://www.bioxfel.org/resources/In-vivo-protein-crystallization-opens
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Structure-factor analysis of femtosecond microdiffraction patterns from protein nanocrystals
28 Feb 2011 | Publications | Contributor(s): X. Wang, A. V. Martin, L. Lomb, T. A. White, A. Barty, F. R. Maia, R. A. Kirian, A. Aquila, Henry Chapman, Petra Fromme, James Holton, Mark S. Hunter, Marius Schmidt, John Spence
A complete set of structure factors has been extracted from hundreds of thousands of femtosecond single-shot X-ray microdiffraction patterns taken from randomly oriented nanocrystals. The method of …
https://www.bioxfel.org/resources/Structure-factor-analysis-of-femtosecond-microdiffraction
