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Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments.

Journal article
Authors Rebecka Andersson
Cecilia Safari
Petra Båth
Robert Bosman
Anastasya Shilova
Peter Dahl
Rasmus Kjeldsen-Jensen
Jie Nan
Robert L Shoeman
Marco Kloos
R Bruce Doak
Uwe Mueller
Richard Neutze
Gisela Brändén
Published in Acta crystallographica. Section D, Structural biology
Volume 75
Issue Pt 10
Pages 937-946
ISSN 2059-7983
Publication year 2019
Published at Department of Chemistry and Molecular Biology
Pages 937-946
Language en
Links dx.doi.org/10.1107/S205979831901269...
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Biophysics, Biochemistry, Structural Biology

Abstract

Serial crystallography is having an increasing impact on structural biology. This emerging technique opens up new possibilities for studying protein structures at room temperature and investigating structural dynamics using time-resolved X-ray diffraction. A limitation of the method is the intrinsic need for large quantities of well ordered micrometre-sized crystals. Here, a method is presented to screen for conditions that produce microcrystals of membrane proteins in the lipidic cubic phase using a well-based crystallization approach. A key advantage over earlier approaches is that the progress of crystal formation can be easily monitored without interrupting the crystallization process. In addition, the protocol can be scaled up to efficiently produce large quantities of crystals for serial crystallography experiments. Using the well-based crystallization methodology, novel conditions for the growth of showers of microcrystals of three different membrane proteins have been developed. Diffraction data are also presented from the first user serial crystallography experiment performed at MAX IV Laboratory.

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Denna text är utskriven från följande webbsida:
http://gu.se/english/research/publication/?publicationId=284525
Utskriftsdatum: 2019-12-12