Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser.
Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser.
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DOI:
10.1103/physrevb.84.214111
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发表时间:
2011-12-01
期刊:
影响因子:
--
通讯作者:
Schlichting I
中科院分区:
文献类型:
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作者:
Lomb L;Barends TR;Kassemeyer S;Aquila A;Epp SW;Erk B;Foucar L;Hartmann R;Rudek B;Rolles D;Rudenko A;Shoeman RL;Andreasson J;Bajt S;Barthelmess M;Barty A;Bogan MJ;Bostedt C;Bozek JD;Caleman C;Coffee R;Coppola N;Deponte DP;Doak RB;Ekeberg T;Fleckenstein H;Fromme P;Gebhardt M;Graafsma H;Gumprecht L;Hampton CY;Hartmann A;Hauser G;Hirsemann H;Holl P;Holton JM;Hunter MS;Kabsch W;Kimmel N;Kirian RA;Liang M;Maia FR;Meinhart A;Marchesini S;Martin AV;Nass K;Reich C;Schulz J;Seibert MM;Sierra R;Soltau H;Spence JC;Steinbrener J;Stellato F;Stern S;Timneanu N;Wang X;Weidenspointner G;Weierstall U;White TA;Wunderer C;Chapman HN;Ullrich J;Strüder L;Schlichting I
X-ray free-electron lasers deliver intense femtosecond pulses that promise to yield high resolution diffraction data of nanocrystals before the destruction of the sample by radiation damage. Diffraction intensities of lysozyme nanocrystals collected at the Linac Coherent Light Source using 2 keV photons were used for structure determination by molecular replacement and analyzed for radiation damage as a function of pulse length and fluence. Signatures of radiation damage are observed for pulses as short as 70 fs. Parametric scaling used in conventional crystallography does not account for the observed effects.