Purification, crystallization and preliminary X-ray analysis of the M.BseCI DNA methyltransferase from Bacillus stearothermophilus.
نویسندگان
چکیده
The DNA methyltransferase M.BseC1 from B. stearothermophilus methylates the N6 atom of the 3' adenine in the sequence 5'-ATCGAT-3'. The 579-residue protein has been isolated and crystallized using seeding and microdialysis techniques. The crystals are monoclinic, space group P2(1) with cell dimensions a = 53.7, b = 85.7, c = 151.8 A and beta = 95.1 degrees, two molecules in the asymmetric unit and diffract to at least 2.5 A resolution.
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ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 53 Pt 4 شماره
صفحات -
تاریخ انتشار 1997