Journal Article

PUBDB-2015-04289

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser

Wu, W. ; Nogly, P. ; Rheinberger, J. ; Kick, L. M. ; Gati, C.>Extern* ; Nelson, G. ; Deupi, X. ; Standfuss, J. ; Schertler, G. ; Panneels, V. (Corresponding author)

2015
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1107/S2053230X15009966

Abstract: 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.

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Research Program(s):

1. 6211 - Extreme States of Matter: From Cold Ions to Hot Plasmas (POF3-621) (POF3-621)
2. NANOMEM - Membrane Protein Nanocrystallography (317079) (317079)

Experiment(s):

1. Experiments at CFEL

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Database coverage:
; ; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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