Crystallization and preliminary crystallographic analysis of RepA1, a replication control protein of the RepFIC replicon of enterotoxin plasmid EntP307.
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 A, b = 67 A, and c = 243 A. They diffract X-rays to 3.3 A resolution and probably contain two 40,000 molecular weight RepA1 molecules per asymmetric unit.
Song
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H
Department of Biochemistry and Molecular Biology, University of Leeds, United Kingdom.
Phillips
S E
SE
Parsons
M R
MR
Maas
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R
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004261:DNA Replication; D004768:Enterotoxins / Q000235:genetics*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D015870:Gene Expression; D008970:Molecular Weight; D010957:Plasmids; D012093:Replicon
D001426:Bacterial Proteins; D004768:Enterotoxins; C070013:REPA1 protein, Bacteria