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@ARTICLE{Lieske:422773,
author = {Lieske, Julia and Cerv, Maximilian and Kreida, Stefan and
Komadina, Dana and Fischer, Janine and Barthelmess, Miriam
and Fischer, Pontus and Pakendorf, Tim and Yefanov,
Oleksandr and Mariani, Valerio and Seine, Thomas and Ross,
Breyan H. and Crosas, Eva and Lorbeer, Olga and Burkhardt,
Anja and Lane, Thomas J. and Guenther, Sebastian and
Bergtholdt, Julian and Schoen, Silvan and
Törnroth-Horsefield, Susanna and Chapman, Henry N. and
Meents, Alke},
title = {{O}n-{C}hip {C}rystallization for {S}erial
{C}rystallopgraphy {E}xperiments and {O}n-{C}hip {L}igand
{B}inding {S}tudies},
journal = {IUCrJ},
volume = {2019},
number = {4},
issn = {2052-2525},
address = {Chester},
reportid = {PUBDB-2019-02326},
pages = {714-728},
year = {2019},
note = {© International Union of Crystallography},
abstract = {Efficient and reliable sample delivery has remained one of
the bottlenecks for serial crystallography experiments.
Compared with other methods, fixed-target sample delivery
offers the advantage of significantly reduced sample
consumption and shorter data collection times owing to
higher hit rates. Here, a new method of on-chip
crystallization is reported which allows the efficient and
reproducible growth of large numbers of protein crystals
directly on micro-patterned silicon chips for in-situ serial
crystallography experiments. Crystals are grown by
sitting-drop vapor diffusion and previously established
crystallization conditions can be directly applied. By
reducing the number of crystal-handling steps, the method is
particularly well suited for sensitive crystal systems.
Excessive mother liquor can be efficiently removed from the
crystals by blotting, and no sealing of the fixed-target
sample holders is required to prevent the crystals from
dehydrating. As a consequence, `naked' crystals are obtained
on the chip, resulting in very low background scattering
levels and making the crystals highly accessible for
external manipulation such as the application of ligand
solutions. Serial diffraction experiments carried out at
cryogenic temperatures at a synchrotron and at room
temperature at an X-ray free-electron laser yielded
high-quality X-ray structures of the human membrane protein
aquaporin 2 and two new ligand-bound structures of
thermolysin and the human kinase DRAK2. The results
highlight the applicability of the method for future
high-throughput on-chip screening of pharmaceutical
compounds.},
cin = {CFEL-I / FS-CFEL-1},
ddc = {530},
cid = {I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)FS-CFEL-1-20120731},
pnm = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
6G3 - PETRA III (POF3-622) / AXSIS - Frontiers in Attosecond
X-ray Science: Imaging and Spectroscopy (609920) / EUCALL -
European Cluster of Advanced Laser Light Sources (654220) /
SWEDEN-DESY - SWEDEN-DESY Collaboration
$(2020_Join2-SWEDEN-DESY)$},
pid = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G3 /
G:(EU-Grant)609920 / G:(EU-Grant)654220 /
$G:(DE-HGF)2020_Join2-SWEDEN-DESY$},
experiment = {EXP:(DE-H253)P-P11-20150101 /
EXP:(DE-H253)CFEL-Exp-20150101 /
EXP:(DE-MLZ)External-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:31316815},
UT = {WOS:000473692700024},
doi = {10.1107/S2052252519007395},
url = {https://bib-pubdb1.desy.de/record/422773},
}