Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli

Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli

The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The s...

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Veröffentlicht in:Journal of molecular biology 1988-04, Vol.200 (4), p.751-752
Hauptverfasser: MOODY, P. C. E, DEMPLE, B
Format: Artikel
Sprache:eng
Schlagworte:
Biological and medical sciences
Crystalline structure
Crystallization
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
Methyltransferases
Molecular biophysics
O-Methylguanine-DNA Methyltransferase
Structure in molecular biology
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Zusammenfassung:The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The space group is P21 with unit cell dimensions a = 46.3 A, b = 45.8 A, c = 46.9 A and beta = 113.3 degrees.
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(88)90488-3