-
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://bioxfel.org/resources/De-novo-protein-crystal-structure
-
The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA
23 Jul 2013 | Publications | Contributor(s): E. J. Grayhack, J. R. Wolfley, E. Quartley, S. Corretore, H. Tsuruta, E. M. Phizicky, Tom Grant, Joseph Luft, Edward Snell
Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended N-terminal domain (NTD) whose precise function is unknown. Although GlnRS structures from two prokaryotic species are known, no …
https://bioxfel.org/resources/The-structure-of-yeast-glutaminyl-tRNA
-
Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser
10 Jan 2013 | Publications | Contributor(s): C. Betzel, K. Nass, G. J. Williams, M. M. Seibert, T. A. White, R. B. Doak, I. Schlichting, D. Rehders, A. Aquila, M. Duszenko, S. Boutet, N. Timneanu, H. Fleckenstein, L. Galli, R. L. Shoeman, T. C. Chao, A. V. Martin, F. Stellato, M. Liang, S. Mogk, R. A. Kirian, I. Grotjohann, D. P. DePonte, S. Bajt, T. R. Barends, N. A. Zatsepin, L. Redecke, C. Caleman, L. C. Johansson, G. Katona, R. Koopmann, T. Barth, A. Barty, J. Steinbrener, D. Wang, M. J. Bogan, S. Kassemeyer, D. Arnlund, L. Lomb, R. Neutze, 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
-
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://bioxfel.org/resources/Small-angle-X-ray-scattering-and-single-molecule
-
Purification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complex
31 Dec 2011 | Publications | Contributor(s): A. L. Stiegler, T. J. Boggon, D. A. Calderwood, Tom Grant, Joseph Luft, Edward Snell
The heterotrimeric protein complex containing the integrin linked kinase (ILK), parvin, and PINCH proteins, termed the IPP complex, is an essential component of focal adhesions, where it interacts …
https://bioxfel.org/resources/Purification-and-SAXS-analysis-of
-
Femtosecond X-ray protein nanocrystallography
02 Feb 2011 | Publications | Contributor(s): A. Rocker, R. G. Sierra, F. Krasniqi, X. Wang, C. D. Schroter, S. Schorb, R. A. Kirian, H. Gorke, K. Nass, M. Barthelmess, J. Andreasson, D. Rolles, T. Gorkhover, B. Rudek, S. Boutet, A. Aquila, G. Potdevin, M. Svenda, J. Ullrich, L. Lomb, I. Andersson, O. Jonsson, C. Y. Hampton, S. W. Epp, A. V. Martin, R. L. Shoeman, F. Schopper, J. Hajdu, R. B. Doak, H. Hirsemann, N. Coppola, L. Foucar, M. J. Bogan, A. Homke, D. Starodub, C. Caleman, S. Marchesini, G. Weidenspointner, M. Adolph, I. Schlichting, D. Pietschner, T. A. White, B. Nilsson, S. Bajt, M. M. Seibert, J. Schulz, L. Gumprecht, N. Timneanu, G. J. Williams, S. Stern, A. Rudenko, R. Hartmann, F. R. Maia, C. Reich, J. D. Bozek, R. Andritschke, H. Graafsma, K. U. Kuhnel, M. Bott, A. Barty, D. Rupp, T. R. Barends, C. Bostedt, S. Herrmann, G. Schaller, L. Struder, I. Grotjohann, P. Holl, D. P. DePonte, B. Erk, R. Neutze, G. Hauser, J. Krzywinski, H. Soltau, N. Kimmel, M. Liang, Henry Chapman, Matthias Frank, Petra Fromme, Stefan Hau-Riege, James Holton, Mark S. Hunter, Mark Messerschmidt, Marius Schmidt, John Spence, Uwe Weierstall
X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the …
https://bioxfel.org/resources/Femtosecond-X-ray-protein-nanocrystallography
