Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser

被引:12
作者
Wu, Wenting [1 ]
Nogly, Przemyslaw [1 ]
Rheinberger, Jan [1 ]
Kick, Leonhard M. [1 ]
Gati, Cornelius [1 ]
Nelson, Garrett [1 ]
Deupi, Xavier [1 ]
Standfuss, Joerg [1 ]
Schertler, Gebhard [1 ]
Panneels, Valerie [1 ]
机构
[1] Paul Scherrer Inst, Lab Biomol Res, CH-5232 Villigen, Switzerland
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷
基金
瑞士国家科学基金会;
关键词
batch crystallization; GPCR; serial crystallography; FEL; dynamics; SERIAL FEMTOSECOND CRYSTALLOGRAPHY; PROTEIN-STRUCTURE DETERMINATION; CRYSTAL-STRUCTURE; COUPLED RECEPTOR; NANOCRYSTALLOGRAPHY; OPPORTUNITIES;
D O I
10.1107/S2053230X15009966
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:856 / 860
页数:5
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