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Updated: Aug 22, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary X-ray analysis of Escherichia coli MutT in binary and ternary complex forms
Teruya Nakamura1, Takefumi Doi, Mutsuo Sekiguchi
1Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, Japan.
Abstract:
During replication, Escherichia coli MutT prevents the misincorporation of mutagenic 8-oxoguanine into nascent DNA strands opposite adenine by hydrolyzing 8-oxo-dGTP in nucleotide pools to 8-oxo-dGMP. E. coli MutT is the most widely investigated member of the Nudix hydrolase family, which is large and found in all organisms. By co-crystallization of MutT with 8-oxo-dGMP, a reaction product, crystals of the binary complex were obtained using ammonium sulfate as a precipitant. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.9, b = 56.0, c = 59.4 A. Assuming the presence of one protein-nucleotide complex in the asymmetric unit, the Matthews coefficient V(M) is 2.1 A(3) Da(-1). Crystals of the ternary complex were prepared by soaking crystals of the binary complex in 1 mM MnCl(2) solution. They diffracted to 1.96 and 2.56 A resolution, respectively.
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