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Acta Crystallogr D Biol Crystallogr. 1997 Jul 01;53:477-9. doi: 10.1107/S0907444997002291.

Purification, crystallization and preliminary X-ray analysis of the M.BseCI DNA methyltransferase from Bacillus stearothermophilus.

Acta crystallographica. Section D, Biological crystallography

A Athanasiadis, Y Papanikolau, M Rina, M Papadovasilaki, Z Dauter, K Petratos, V Bouriotis, M Kokkinidis

Affiliations

  1. University of Crete, Department of Biology, Greece.

PMID: 15299919 DOI: 10.1107/S0907444997002291

Abstract

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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