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De novo protein crystal structure determination from X-ray free-electron laser data
08 Jan 2014 | Publications | Contributor(s): R. B. Doak, K. Nass, G. J. Williams, S. Botha, T. R. Barends, J. E. Koglin, R. L. Shoeman, L. Foucar, I. Schlichting, S. Boutet, 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://bioxfel.org/resources/De-novo-protein-crystal-structure
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Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser
10 Jan 2013 | Publications | Contributor(s): M. J. Bogan, S. Kassemeyer, L. Lomb, D. Arnlund, R. Neutze, G. J. Williams, C. Betzel, K. Nass, R. B. Doak, M. M. Seibert, T. A. White, A. Aquila, I. Schlichting, D. Rehders, M. Duszenko, S. Boutet, N. Timneanu, H. Fleckenstein, L. Galli, T. C. Chao, R. L. Shoeman, F. Stellato, A. V. Martin, R. A. Kirian, M. Liang, S. Mogk, T. R. Barends, I. Grotjohann, D. P. DePonte, L. Redecke, S. Bajt, N. A. Zatsepin, G. Katona, C. Caleman, L. C. Johansson, R. Koopmann, T. Barth, A. Barty, J. Steinbrener, D. Wang, Henry Chapman, Matthias Frank, Petra Fromme, Mark S. Hunter, Christopher Kupitz, Mark Messerschmidt, John Spence, Uwe Weierstall
https://bioxfel.org/resources/Natively-Inhibited-Trypanosoma-brucei-Cathepsin
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Breaking the radiation damage limit with Cryo-SAXS
07 Jan 2013 | Publications | Contributor(s): M. Warkentin, H. Chen, R. E. Thorne, R. E. Gillilan, J. B. Hopkins, S. P. Meisburger, Lois Pollack
Small angle x-ray scattering (SAXS) is a versatile and widely used technique for obtaining low-resolution structures of macromolecules and complexes. SAXS experiments measure molecules in solution, …
https://bioxfel.org/resources/Breaking-the-radiation-damage-limit
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High-resolution protein structure determination by serial femtosecond crystallography
19 Jul 2012 | Publications | Contributor(s): L. J. Koerner, R. A. Kirian, G. Katona, P. A. Montanez, M. Liang, F. Stellato, C. Caleman, T. R. Barends, J. Morse, N. A. Zatsepin, L. Redecke, R. Herbst, A. Aquila, S. Kassemeyer, D. P. DePonte, L. C. Johansson, M. W. Tate, G. J. Williams, C. Y. Hampton, W. Ghonsalves, J. Steinbrener, R. Neutze, N. van Bakel, M. J. Bogan, D. Wang, A. V. Martin, T. A. White, J. Defever, L. Lomb, R. B. Doak, S. Boutet, H. T. Philipp, D. Arnlund, K. Nass, P. Hart, M. M. Seibert, G. Haller, C. Kenney, J. Pines, N. Timneanu, M. Hromalik, R. L. Shoeman, A. Barty, S. M. Gruner, I. Schlichting, D. Schafer, Henry Chapman, Petra Fromme, Mark S. Hunter, Christopher Kupitz, Mark Messerschmidt, John Spence, Uwe Weierstall
Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding …
https://bioxfel.org/resources/High-resolution-protein-structure-determination-by
