Literature DB >> 10216311

Crystallization and preliminary X-ray crystallographic studies of RepDC, a hybrid rolling-circle plasmid replication initiator protein.

D E Klimenko1, M A Convery, S Rowsell, C D Thomas, S E Phillips.   

Abstract

The hybrid plasmid-replication initiator protein RepDC, which is a fusion of the catalytic fragment of the RepD protein and the DNA-binding fragment of the RepC protein from Staphylococcus aureus, has been successfully crystallized and X-ray data to 3.5 A have been collected on a synchrotron radiation source. Crystals belong to space group I4132 with unit-cell dimensions a = b = c = 165.1 A. The crystals are estimated to contain one protein monomer per asymmetric unit, with 55% solvent content.

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Year:  1999        PMID: 10216311     DOI: 10.1107/s0907444999003005

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Identification, characterization and preliminary X-ray diffraction analysis of the rolling-circle replication initiator protein from plasmid pSTK1.

Authors:  Stephen B Carr; Lauren B Mecia; Simon E V Phillips; Christopher D Thomas
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-09-28

2.  Structures of replication initiation proteins from staphylococcal antibiotic resistance plasmids reveal protein asymmetry and flexibility are necessary for replication.

Authors:  Stephen B Carr; Simon E V Phillips; Christopher D Thomas
Journal:  Nucleic Acids Res       Date:  2016-01-20       Impact factor: 16.971

  2 in total

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