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@ARTICLE{Schmidt:639478,
author = {Schmidt, Christina and Lorenzen, Kristina and Schulz,
Joachim and Han, Huijong},
title = {{S}tandard {S}ample {P}reparation for {S}erial
{F}emtosecond {C}rystallography},
journal = {Biomolecules},
volume = {15},
number = {11},
issn = {2218-273X},
address = {Basel},
publisher = {MDPI},
reportid = {PUBDB-2025-04564},
pages = {1488},
year = {2025},
abstract = {AbstractThe development of serial crystallography (SX),
including serial synchrotron crystallography (SSX) at
synchrotron sources and serial femtosecond crystallography
(SFX) at X-ray free-electron lasers (XFELs), has facilitated
the collection of high-resolution diffraction data from
micron-sized crystals, providing unique insights into the
structures and dynamics of biomolecules at room temperature.
Standard samples are essential for the commissioning of new
XFEL instruments and the validation of experimental setups.
In this review, we summarize currently used standard
proteins and describe representative microcrystal
preparation workflows for four widely adopted models,
lysozyme, myoglobin, iq-mEmerald, and photoactive yellow
protein (PYP), drawing on established methodologies and
accumulated experience from their applications at the
European XFEL. By consolidating existing knowledge and
integrating protocols that have been systematically refined
and optimized through our experimental efforts, this review
aims to provide practical guidance for the serial
crystallography community, thereby enhancing reproducibility
and ensuring consistent experimental performance across
facilities.Keywords:serial femtosecond crystallography;
microcrystals; standard samples; protocol},
cin = {$XFEL_E2_SEC$},
ddc = {570},
cid = {$I:(DE-H253)XFEL_E2_SEC-20210408$},
pnm = {6G13 - Accelerator of European XFEL (POF4-6G13)},
pid = {G:(DE-HGF)POF4-6G13},
experiment = {EXP:(DE-H253)XFEL(machine)-20150101},
typ = {PUB:(DE-HGF)16},
doi = {10.3390/biom15111488},
url = {https://bib-pubdb1.desy.de/record/639478},
}