%0 Journal Article
%A Wu, Wenting
%A Nogly, Przemyslaw
%A Rheinberger, Jan
%A Kick, Leonhard M.
%A Gati, Cornelius
%A Nelson, Garrett
%A Deupi, Xavier
%A Standfuss, Jörg
%A Schertler, Gebhard
%A Panneels, Valérie
%T Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser
%J Acta crystallographica / F
%V 71
%N 7
%@ 2053-230X
%C Oxford [u.a.]
%I Blackwell
%M PUBDB-2015-04289
%P 856 - 860
%D 2015
%X Rhodopsin is a membrane protein from the G protein-coupled receptor family. Together with its ligand retinal, it forms the visual pigment responsible for night vision. In order to perform ultrafast dynamics studies, a time-resolved serial femtosecond crystallography method is required owing to the nonreversible activation of rhodopsin. In such an approach, microcrystals in suspension are delivered into the X-ray pulses of an X-ray free-electron laser (XFEL) after a precise photoactivation delay. Here, a millilitre batch production of high-density microcrystals was developed by four methodical conversion steps starting from known vapour-diffusion crystallization protocols: (i) screening the low-salt crystallization conditions preferred for serial crystallography by vapour diffusion, (ii) optimization of batch crystallization, (iii) testing the crystal size and quality using second-harmonic generation (SHG) imaging and X-ray powder diffraction and (iv) production of millilitres of rhodopsin crystal suspension in batches for serial crystallography tests; these crystals diffracted at an XFEL at the Linac Coherent Light Source using a liquid-jet setup.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000357830700008
%R 10.1107/S2053230X15009966
%U https://bib-pubdb1.desy.de/record/275872