A. Athanasiadis et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE M.BSECI DNA METHYLTRANSFERASE FROM BACILLUS-STEAROTHERMOPHILUS, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 477-479
Citations number
26
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
The DNA methyltransferase M.BseC1 from B. stearothermophilus methylate
s 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 m
icrodialysis techniques. The crystals are monoclinic, space group P2(1
) with cell dimensions a = 53.7, b = 85.7, c = 1518 Angstrom and beta
= 95.1 degrees, two molecules in the asymmetric unit and diffract to a
t least 2.5 Angstrom resolution.