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Crystallization and preliminary crystallographic analysis of RepA1, a replication control protein of the RepFIC replicon of enterotoxin plasmid EntP307
Author(s) -
Song Haiwei,
Phillips Simon E.V.,
Parsons Mark R.,
Maas Renata
Publication year - 1996
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(199605)25:1<137::aid-prot13>3.0.co;2-l
Subject(s) - replicon , plasmid , crystallization , enterotoxin , crystallography , replication (statistics) , origin of replication , resolution (logic) , molecule , chemistry , biology , microbiology and biotechnology , dna , genetics , escherichia coli , gene , virology , organic chemistry , artificial intelligence , computer science
RepA1 protein is essential for replication of the RepFIC replicon of enterotoxin plasmid EntP307 and is thought to interact directly with the origin of replication. We have purified RepA1 from an over‐producing expression system and have prepared single crystals using a macroseeding technique. The crystals belong to space group P2 1 2 1 2 1 or P2 1 2 1 2, with cell dimensions a = 61 Å, b = 67 Å, and c = 243 Å. They diffract X‐rays to 3.3 Å resolution and probably contain two 40,000 molecular weight RepA1 molecules per asymmetric unit. © 1996 Wiley‐Liss, Inc.