TY  - JOUR
AU  - Lieske, Julia
AU  - Cerv, Maximilian
AU  - Kreida, Stefan
AU  - Komadina, Dana
AU  - Fischer, Janine
AU  - Barthelmess, Miriam
AU  - Fischer, Pontus
AU  - Pakendorf, Tim
AU  - Yefanov, Oleksandr
AU  - Mariani, Valerio
AU  - Seine, Thomas
AU  - Ross, Breyan H.
AU  - Crosas, Eva
AU  - Lorbeer, Olga
AU  - Burkhardt, Anja
AU  - Lane, Thomas J.
AU  - Guenther, Sebastian
AU  - Bergtholdt, Julian
AU  - Schoen, Silvan
AU  - Törnroth-Horsefield, Susanna
AU  - Chapman, Henry N.
AU  - Meents, Alke
TI  - On-Chip Crystallization for Serial Crystallopgraphy Experiments and On-Chip Ligand Binding Studies
JO  - IUCrJ
VL  - 2019
IS  - 4
SN  - 2052-2525
CY  - Chester
M1  - PUBDB-2019-02326
SP  - 714-728
PY  - 2019
N1  - © International Union of Crystallography
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:31316815
UR  - <Go to ISI:>//WOS:000473692700024
DO  - DOI:10.1107/S2052252519007395
UR  - https://bib-pubdb1.desy.de/record/422773
ER  -