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Strategy for membrane protein crystallization exemplified with OmpA and OmpX
Author(s) -
Pautsch Alex,
Vogt Joachim,
Model Kirstin,
Siebold Christian,
Schulz Georg E.
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19990201)34:2<167::aid-prot2>3.0.co;2-h
Subject(s) - bacterial outer membrane , crystallization , membrane protein , membrane , resolution (logic) , chemistry , biology , microbiology and biotechnology , crystallography , biochemistry , escherichia coli , computer science , gene , organic chemistry , artificial intelligence
The bacterial outer membrane proteins OmpA and OmpX were modified in such a manner that they yielded bulky crystals diffracting X‐rays isotropically beyond 2 Å resolution and permitting detailed structural analyses. The procedure involved semi‐directed mutagenesis, mass production into inclusion bodies, and (re)naturation therefrom; it should be applicable for a broader range of membrane proteins. Proteins 1999;34:167–172. © 1999 Wiley‐Liss, Inc.