Open AccessPurification, crystallization and preliminary X‐ray analysis of the Bse CI DNA methyltransferase from Bacillus stearothermophilus in complex with its cognate DNA
Author(s) -
Kapetaniou Evangelia G.,
Kotsifaki Dina,
Providaki Mary,
Rina Maria,
Bouriotis Vassilis,
Kokkinidis Michael
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106051530
Subject(s) - geobacillus stearothermophilus , dna , dna methyltransferase , methyltransferase , crystallography , crystallization , resolution (logic) , molecule , enzyme , chemistry , stereochemistry , biology , biochemistry , methylation , thermophile , organic chemistry , artificial intelligence , computer science
The DNA methyltransferase M. Bse CI 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. Bse CI was crystallized in complex with its cognate DNA. The crystals were found to belong to the hexagonal space group P 6, with unit‐cell parameters a = b = 87.0, c = 156.1 Å, β = 120.0° and one molecule in the asymmetric unit. Two complete data sets were collected at wavelengths of 1.1 and 2.0 Å to 2.5 and 2.8 Å resolution, respectively, using synchrotron radiation at 100 K.