Ontology highlight
ABSTRACT:
SUBMITTER: Boutet S
PROVIDER: S-EPMC3788707 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Boutet Sébastien S Lomb Lukas L Williams Garth J GJ Barends Thomas R M TR Aquila Andrew A Doak R Bruce RB Weierstall Uwe U DePonte Daniel P DP Steinbrener Jan J Shoeman Robert L RL Messerschmidt Marc M Barty Anton A White Thomas A TA Kassemeyer Stephan S Kirian Richard A RA Seibert M Marvin MM Montanez Paul A PA Kenney Chris C Herbst Ryan R Hart Philip P Pines Jack J Haller Gunther G Gruner Sol M SM Philipp Hugh T HT Tate Mark W MW Hromalik Marianne M Koerner Lucas J LJ van Bakel Niels N Morse John J Ghonsalves Wilfred W Arnlund David D Bogan Michael J MJ Caleman Carl C Fromme Raimund R Hampton Christina Y CY Hunter Mark S MS Johansson Linda C LC Katona Gergely G Kupitz Christopher C Liang Mengning M Martin Andrew V AV Nass Karol K Redecke Lars L Stellato Francesco F Timneanu Nicusor N Wang Dingjie D Zatsepin Nadia A NA Schafer Donald D Defever James J Neutze Richard R Fromme Petra P Spence John C H JC Chapman Henry N HN Schlichting Ilme I
Science (New York, N.Y.) 20120531 6092
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 s ...[more]