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 radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

Boutet, S., Lomb, L., Williams, G.j., Barends, T., Aquila, A., Doak, R.b., et al. (2012). High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography. SCIENCE, 337(6092), 362-364 [10.1126/science.1217737].

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Stellato F.;
2012-01-01

Abstract

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 radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
2012
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore FIS/07
English
Con Impact Factor ISI
Boutet, S., Lomb, L., Williams, G.j., Barends, T., Aquila, A., Doak, R.b., et al. (2012). High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography. SCIENCE, 337(6092), 362-364 [10.1126/science.1217737].
Boutet, S; Lomb, L; Williams, Gj; Barends, Trm; Aquila, A; Doak, Rb; Weierstall, U; Deponte, Dp; Steinbrener, J; Shoeman, Rl; Messerschmidt, M; Barty, A; White, Ta; Kassemeyer, S; Kirian, Ra; Seibert, Mm; Montanez, Pa; Kenney, C; Herbst, R; Hart, P; Pines, J; Haller, G; Gruner, Sm; Philipp, Ht; Tate, Mw; Hromalik, M; Koerner, Lj; Van Bakel, N; Morse, J; Ghonsalves, W; Arnlund, D; Bogan, Mj; Caleman, C; Fromme, R; Hampton, Cy; Hunter, Ms; Johansson, Lc; Katona, G; Kupitz, C; Liang, M; Martin, Av; Nass, K; Redecke, L; Stellato, F; Timneanu, N; Wang, D; Zatsepin, Na; Schafer, D; Defever, J; Neutze, R; Fromme, P; Spence, Jch; Chapman, Hn; Schlichting, I
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/354245
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