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Well‐based crystallization of lipidic cubic phase microcrystals for serial X‐ray crystallography experiments
Author(s) -
Andersson Rebecka,
Safari Cecilia,
Båth Petra,
Bosman Robert,
Shilova Anastasya,
Dahl Peter,
Ghosh Swagatha,
Dunge Andreas,
Kjeldsen-Jensen Rasmus,
Nan Jie,
Shoeman Robert L.,
Kloos Marco,
Doak R. Bruce,
Mueller Uwe,
Neutze Richard,
Brändén Gisela
Publication year - 2019
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798319012695
Subject(s) - crystallization , diffraction , crystallography , x ray crystallography , phase (matter) , protein crystallization , materials science , crystal (programming language) , chemical physics , chemistry , computer science , physics , optics , organic chemistry , programming language
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.