TY  - JOUR
AU  - Chavas, Leonard
AU  - Gumprecht, L.
AU  - Chapman, H. N.
TI  - Possibilities for serial femtosecond crystallography sample delivery at future light sources
JO  - Structural dynamics
VL  - 2
IS  - 4
SN  - 2329-7778
CY  - Melville, NY
PB  - AIP Publishing LLC
M1  - PUBDB-2015-04292
SP  - 041709 -
PY  - 2015
AB  - Serial femtosecond crystallography (SFX) uses X-ray pulses from free-electron laser(FEL) sources that can outrun radiation damage and thereby overcome long-standing limits in the structure determination of macromolecular crystals. Intense X-rayFEL pulses of sufficiently short duration allow the collection of damage-free data at room temperature and give the opportunity to study irreversible time-resolved events. SFX may open the way to determine the structure of biological molecules that fail to crystallize readily into large well-diffracting crystals. Taking advantage of FELs with high pulse repetition rates could lead to short measurement times of just minutes. Automated delivery of sample suspensions for SFX experiments could potentially give rise to a much higher rate of obtaining complete measurements than at today's third generation synchrotron radiation facilities, as no crystal alignment or complex robotic motions are required. This capability will also open up extensive time-resolved structural studies. New challenges arise from the resulting high rate of data collection, and in providing reliable sample delivery. Various developments for fully automated high-throughput SFX experiments are being considered for evaluation, including new implementations for a reliable yet flexible sample environment setup. Here, we review the different methods developed so far that best achieve sample delivery for X-rayFEL experiments and present some considerations towards the goal of high-throughput structure determination with X-rayFELs.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000360649200011
C6  - pmid:26798808
DO  - DOI:10.1063/1.4921220
UR  - https://bib-pubdb1.desy.de/record/275875
ER  -