Purification, crystallization and preliminary X-ray analysis of the BseCI DNA methyltransferase from Bacillus stearothermophilus in complex with its cognate DNA.
The DNA methyltransferase M.BseCI from Bacillus stearothermophilus (EC 2.1.1.72), a 579-amino-acid enzyme, methylates the N6 atom of the 3' adenine in the sequence 5'-ATCGAT-3'. M.BseCI was crystallized in complex with its cognate DNA. The crystals were found to belong to the hexagonal space group P6, with unit-cell parameters a = b = 87.0, c = 156.1 A, beta = 120.0 degrees and one molecule in the asymmetric unit. Two complete data sets were collected at wavelengths of 1.1 and 2.0 A to 2.5 and 2.8 A resolution, respectively, using synchrotron radiation at 100 K.
Kapetaniou
Evangelia G
EG
Institute of Molecular Biology and Biotechnology, PO Box 1527, GR-71110, Heraklion, Crete, Greece.
Kotsifaki
Dina
D
Providaki
Mary
M
Rina
Maria
M
Bouriotis
Vassilis
V
Kokkinidis
Michael
M
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004269:DNA, Bacterial / Q000737:chemistry / Q000302:isolation & purification*; D001411:Geobacillus stearothermophilus / Q000737:chemistry / Q000302:isolation & purification*; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000737:chemistry* / Q000302:isolation & purification*
D004269:DNA, Bacterial; C061926:DNA modification methylase Cla I; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)