TY  - JOUR
AU  - Chapman, H. N.
AU  - Caleman, C.
AU  - Timneanu, N.
TI  - Diffraction before destruction
JO  - Philosophical transactions of the Royal Society of London / B
VL  - 369
IS  - 1647
SN  - 1471-2970
CY  - London
PB  - JSTOR
M1  - DESY-2014-02888
SP  - 20130313
PY  - 2014
AB  - X-ray free-electron lasers have opened up the possibility of structure determination of protein crystals at room temperature, free of radiation damage. The femtosecond-duration pulses of these sources enable diffraction signals to becollected from samples at doses of 1000 MGy or higher. The sample is vaporized by the intense pulse, but not before the scattering that gives rise to the diffraction pattern takes place. Consequently, only a single flash diffraction pattern can be recorded from a crystal, giving rise to the method of serial crystallography where tens of thousands of patterns are ollected from individual crystals that flow across the beam and the patterns are indexed and aggregated into a set of structure factors. The high-dose tolerance and the many-crystal averaging approach allow data to be collected from much smaller crystals than have been examined at synchrotron radiation facilities, even from radiation-sensitive samples. Here, we review the interaction of intense femtosecond X-ray pulses with materials and discuss the implications forstructure determination. We identify various dose regimes and conclude that the strongest achievable signals for a given sample are attained at the highest possible dose rates, from highest possible pulse intensities.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000337367600003
C6  - pmid:24914146
DO  - DOI:10.1098/rstb.2013.0313
UR  - https://bib-pubdb1.desy.de/record/169302
ER  -