title: Cloning, expression, and purification of Bacillus stearothermophilus DNA primase and crystallization of the zinc-binding domain.
abstract: The dnaG gene encoding DNA primase has been isolated from chromosomal DNA of Bacillus stearothermophilus and its entire nucleotide sequence determined. The deduced amino acid sequence comprised 597 amino acid residues and the molecular mass was calculated to be 67068 Da. B. stearothermophilus primase was overexpressed in Escherichia coli and purified to homogeneity. The N-terminal 12 kDa zinc-binding domain has been crystallized. The crystals are of the monoclinic space group P21 with cell dimensions a=36 A, b=59 A, c=46 A, beta=91.8 degrees and diffract to 1.7 A resolution.
authors: Sir William Dunn School of Pathology, University of Oxford, South Park Road, Oxford OX1 3RE, UK.
authors: H
authors: H
authors: Pan
authors: L E
authors: LE
authors: Bird
authors: D B
authors: DB
authors: Wigley
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D019915:DNA Primase / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D001411:Geobacillus stearothermophilus / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data
chemical_list: D002352:Carrier Proteins; C017800:zinc-binding protein; D019915:DNA Primase