Literature DB >> 8727327

Crystallization and preliminary crystallographic analysis of RepA1, a replication control protein of the RepFIC replicon of enterotoxin plasmid EntP307.

H Song1, S E Phillips, M R Parsons, R Maas.   

Abstract

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.

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Year:  1996        PMID: 8727327     DOI: 10.1002/(SICI)1097-0134(199605)25:1<137::AID-PROT13>3.0.CO;2-L

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  2 in total

1.  Interactions of the RepA1 protein with its replicon targets: two opposing roles in control of plasmid replication.

Authors:  R Maas; C Wang; W K Maas
Journal:  J Bacteriol       Date:  1997-06       Impact factor: 3.490

2.  Role of the RepA1 protein in RepFIC plasmid replication.

Authors:  R Maas; C Wang
Journal:  J Bacteriol       Date:  1997-04       Impact factor: 3.490

  2 in total

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