Purification, crystallization and preliminary X-ray analysis of the M.BseCI DNA methyltransferase from Bacillus stearothermophilus.
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.
Athanasiadis
A
A
University of Crete, Department of Biology, Greece.
Papanikolau
Y
Y
Rina
M
M
Papadovasilaki
M
M
Dauter
Z
Z
Petratos
K
K
Bouriotis
V
V
Kokkinidis
M
M