High-resolution protein structure determination by serial femtosecond crystallography
- Boutet, S.
- Lomb, L.
- Williams, G.
- Barends, T.
- Aquila, A.
- Doak, R.
- Weierstall, U.
- DePonte, D.
- Steinbrener, J.
- Shoeman, R.
- Messerschmidt, M.
- Barty, A.
- White, T.
- Kassemeyer, S.
- Kirian, R.
- Seibert, M.
- Montanez, P.
- Kenney, C.
- Herbst, R.
- Hart, P.
- Pines, J.
- Haller, G.
- Gruner, S.
- Philipp, H.
- Tate, M.
- Hromalik, M.
- Koerner, L.
- van Bakel, N.
- Morse, J.
- Ghonsalves, W.
- Arnlund, D.
- Bogan, M.
- Caleman, C.
- Fromme, R.
- Hampton, C.
- Hunter, M.
- Johansson, L.
- Katona, G.
- Kupitz, C.
- Liang, M.
- Martin, A.
- Nass, K.
- Redecke, L.
- Stellato, F.
- Timneanu, N.
- Wang, D.
- Zatsepin, N.
- Schafer, D.
- Defever, J.
- Neutze, R.
- Fromme, P.
- Spence, J.
- Chapman, H.
- Schlichting, I.
Publication date
July 2012
DOI Publisher
American Association for the Advancement of Science (AAAS)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 (<1×1×3 μm(3)) 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 molecule
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