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High-resolution protein structure determination by serial femtosecond crystallography.

Authors :
Boutet S
Lomb L
Williams GJ
Barends TR
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 JC
Chapman HN
Schlichting I
Source :
Science (New York, N.Y.) [Science] 2012 Jul 20; Vol. 337 (6092), pp. 362-4. Date of Electronic Publication: 2012 May 31.
Publication Year :
2012

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.

Details

Language :
English
ISSN :
1095-9203
Volume :
337
Issue :
6092
Database :
MEDLINE
Journal :
Science (New York, N.Y.)
Publication Type :
Academic Journal
Accession number :
22653729
Full Text :
https://doi.org/10.1126/science.1217737