| Literature DB >> 10095067 |
H Pan1, L E Bird, D B Wigley.
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.Entities:
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Year: 1999 PMID: 10095067 DOI: 10.1016/s0167-4781(99)00025-1
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002