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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/238

Protein structural ensembles are revealed by redefining X-ray electron density noise

06 Jan 2014 | Publications | Contributor(s): T. Alber, J. S. Fraser, P. T. Lang, 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/282

Serial femtosecond crystallography of G protein-coupled receptors

19 Dec 2013 | Publications | Contributor(s): W. Liu, R. C. Stevens, M. Caffrey, D. Wang, R. A. Kirian, S. Boutet, C. Wang, I. Grotjohann, K. R. Beyerlein, G. W. Han, A. Barty, T. A. White, D. Wacker, S. Basu, C. Gati, M. M. Seibert, V. Katritch, K. N. Rendek, G. J. Williams, S. T. Shah, N. A. Zatsepin, J. E. Koglin, Henry Chapman, Vadim Cherezov, Petra Fromme, James Holton, Christopher Kupitz, Applications Manager, Mark Messerschmidt, Garrett Charles Nelson, John Spence, Uwe Weierstall

X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and …

https://www.bioxfel.org/resources/290

The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA

23 Jul 2013 | Publications | Contributor(s): E. M. Phizicky, E. J. Grayhack, J. R. Wolfley, E. Quartley, S. Corretore, H. Tsuruta, 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://www.bioxfel.org/resources/301

Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature

25 Apr 2013 | Publications | Contributor(s): R. J. Gildea, U. Bergmann, J. Messinger, D. W. Schafer, A. Miahnahri, S. Gul, P. H. Zwart, J. Hattne, D. Difiore, M. M. Seibert, R. W. Grosse-Kunstleve, N. K. Sauter, W. E. White, A. Zouni, J. Yano, G. J. Williams, T. C. Weng, R. G. Sierra, J. Kern, D. Sokaras, A. Lampe, S. Boutet, P. Glatzel, C. Glockner, M. J. Latimer, J. E. Koglin, R. Tran, N. Echols, V. K. Yach, A. R. Fry, J. Sellberg, G. Han, S. Koroidov, R. Alonso-Mori, J. Hellmich, D. Milathianaki, P. D. Adams, B. Lassalle-Kaiser, M. J. Bogan, H. Laksmono, Mark Messerschmidt, Ranga Setlur

Intense femtosecond x-ray pulses produced at the Linac Coherent Light Source (LCLS) were used for simultaneous x-ray diffraction (XRD) and x-ray emission spectroscopy (XES) of microcrystals of …

https://www.bioxfel.org/resources/293

Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser

10 Jan 2013 | Publications | Contributor(s): C. Betzel, M. J. Bogan, K. Nass, S. Kassemeyer, G. J. Williams, I. Schlichting, R. Neutze, D. Rehders, A. Aquila, H. Fleckenstein, R. B. Doak, M. M. Seibert, L. Galli, T. A. White, A. V. Martin, M. Duszenko, S. Boutet, F. Stellato, N. Timneanu, T. R. Barends, T. C. Chao, I. Grotjohann, R. L. Shoeman, D. P. DePonte, R. A. Kirian, C. Caleman, M. Liang, L. C. Johansson, S. Mogk, G. Katona, A. Barty, L. Redecke, J. Steinbrener, S. Bajt, D. Wang, N. A. Zatsepin, R. Koopmann, D. Arnlund, L. Lomb, T. Barth, Henry Chapman, Matthias Frank, Petra Fromme, Mark S. Hunter, Christopher Kupitz, Mark Messerschmidt, John Spence, Uwe Weierstall

https://www.bioxfel.org/resources/273

High-resolution protein structure determination by serial femtosecond crystallography

19 Jul 2012 | Publications | Contributor(s): M. M. Seibert, S. Boutet, K. Nass, P. Hart, I. Schlichting, D. Schafer, A. Barty, R. L. Shoeman, N. Timneanu, M. Hromalik, G. Katona, S. M. Gruner, L. J. Koerner, R. A. Kirian, C. Caleman, J. Morse, F. Stellato, P. A. Montanez, M. Liang, D. P. DePonte, A. Aquila, R. Herbst, N. A. Zatsepin, T. R. Barends, L. Redecke, C. Y. Hampton, J. Steinbrener, G. J. Williams, M. W. Tate, S. Kassemeyer, L. C. Johansson, A. V. Martin, J. Defever, D. Wang, R. Neutze, N. van Bakel, W. Ghonsalves, M. J. Bogan, H. T. Philipp, D. Arnlund, T. A. White, L. Lomb, R. B. Doak, C. Kenney, J. Pines, G. Haller, 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://www.bioxfel.org/resources/254

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): J. Hinshaw, T. Y. Yoo, G. Haran, T. R. Sosnick, K. Plaxco, S. P. Meisburger, 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/297

In vivo protein crystallization opens new routes in structural biology

29 Feb 2012 | Publications | Contributor(s): J. Schulz, H. Hirsemann, S. Stern, L. Redecke, R. B. Doak, F. Stellato, C. Bostedt, A. Barty, M. Liang, S. Bajt, L. Foucar, P. Holl, J. D. Bozek, D. Rehders, B. Rudek, H. Graafsma, N. Coppola, T. A. White, M. Barthelmess, R. Hartmann, A. Rudenko, G. J. Williams, C. Reich, S. Kassemeyer, L. Lomb, R. A. Kirian, J. Hajdu, F. R. Maia, C. Betzel, A. Aquila, M. J. Bogan, R. L. Shoeman, K. Nass, N. Timneanu, J. Andreasson, T. Stehle, B. Erk, H. Fleckenstein, D. P. Deponte, J. Ullrich, H. Soltau, S. W. Epp, L. Struder, R. G. Sierra, A. Hartmann, G. Hauser, C. Caleman, M. M. Seibert, S. Boutet, L. Gumprecht, J. Davidsson, X. Wang, D. Rolles, C. B. Wunderer, K. Cupelli, N. Kimmel, I. Schlichting, T. Ekeberg, M. Duszenko, R. Koopmann, A. V. Martin, G. Weidenspointner, C. Y. Hampton, 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/258

Purification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complex

31 Dec 2011 | Publications | Contributor(s): D. A. Calderwood, A. L. Stiegler, T. J. Boggon, 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://www.bioxfel.org/resources/283

Femtosecond X-ray protein nanocrystallography

02 Feb 2011 | Publications | Contributor(s): L. Gumprecht, T. A. White, G. J. Williams, N. Timneanu, S. Bajt, J. Schulz, M. M. Seibert, D. Rupp, C. Bostedt, A. Barty, K. U. Kuhnel, R. Hartmann, J. D. Bozek, M. Bott, H. Graafsma, R. Andritschke, S. Stern, D. P. DePonte, B. Erk, G. Hauser, I. Grotjohann, L. Struder, T. R. Barends, G. Schaller, P. Holl, S. Herrmann, A. Rocker, F. Krasniqi, C. D. Schroter, N. Kimmel, R. Neutze, J. Krzywinski, M. Liang, H. Soltau, D. Rolles, B. Rudek, A. Aquila, K. Nass, R. G. Sierra, J. Andreasson, M. Barthelmess, X. Wang, H. Gorke, R. A. Kirian, S. Schorb, A. V. Martin, F. Schopper, C. Y. Hampton, I. Andersson, L. Lomb, T. Gorkhover, G. Potdevin, O. Jonsson, S. Boutet, J. Ullrich, M. Svenda, A. Homke, D. Starodub, C. Caleman, L. Foucar, N. Coppola, R. L. Shoeman, J. Hajdu, M. J. Bogan, H. Hirsemann, R. B. Doak, S. W. Epp, D. Pietschner, B. Nilsson, I. Schlichting, M. Adolph, G. Weidenspointner, S. Marchesini, A. Rudenko, F. R. Maia, C. Reich, 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://www.bioxfel.org/resources/252