Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli

Peter C.E. Moody; Bruce Demple

doi:10.1016/0022-2836(88)90488-3

Crystallization of O⁶-methylguanine-DNA methyltransferase from Escherichia coli

Peter C.E. Moody
, Bruce Demple

Pharmacological Sciences

Imperial College London

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

The 19,000 M_r 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 Å (1 Å = 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 β = 113.3 °.

Original language	English
Pages (from-to)	751-752
Number of pages	2
Journal	Journal of Molecular Biology
Volume	200
Issue number	4
DOIs	https://doi.org/10.1016/0022-2836(88)90488-3
State	Published - Apr 20 1988

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title = "Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli",

abstract = "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 {\AA} (1 {\AA} = 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 β = 113.3 °.",

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T1 - Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli

AU - Moody, Peter C.E.

AU - Demple, Bruce

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N2 - 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 Å (1 Å = 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 β = 113.3 °.

AB - 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 Å (1 Å = 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 β = 113.3 °.

UR - https://www.scopus.com/pages/publications/0024292506

U2 - 10.1016/0022-2836(88)90488-3

DO - 10.1016/0022-2836(88)90488-3

M3 - Article

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SP - 751

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JF - Journal of Molecular Biology

IS - 4

ER -

Crystallization of O⁶-methylguanine-DNA methyltransferase from Escherichia coli

Abstract

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