Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae.

Ah Reum Han, Hyun Sook Kim, Gye Yoon Cho, Ho Sam Ki, Hwa Young Kim, Kwang Yeon Hwang

Acta crystallographica. Section F, Structural biology and crystallization communications 2012 May 01

filter terms:

Methionine sulfoxide reductase (Msr) is a repair enzyme that reduces oxidized methionine to methionine. The Msr enzyme is divided into MsrA and MsrB, which reduce the S and R configurations of the substrate, respectively. In some pathogenic bacteria MsrA and MsrB exist in a fusion-protein form, MsrAB. In this study, the recombinant MsrA part of MsrAB from Haemophilus influenzae (HIMsrA) was overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. A diffraction data set was collected to 1.6 Å resolution. The crystal of HIMsrA was found to belong to space group P4(1)2(1)2, with unit-cell parameters a = b = 57.29, c = 186.28 Å, a calculated Matthews coefficient of 1.82 Å(3) Da(-1) and two molecules per asymmetric unit. A preliminary solution was determined by molecular replacement. Refinement of the structure is currently in progress.

Citation

Ah Reum Han, Hyun Sook Kim, Gye Yoon Cho, Ho Sam Ki, Hwa Young Kim, Kwang Yeon Hwang. Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae. Acta crystallographica. Section F, Structural biology and crystallization communications. 2012 May 01;68(Pt 5):557-9