Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzae
Author(s) -
Han Ah Reum,
Kim Hyun Sook,
Cho Gye Yoon,
Ki Ho Sam,
Kim HwaYoung,
Hwang Kwang Yeon
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112011256
Subject(s) - msra , methionine , crystallography , methionine sulfoxide , crystallization , chemistry , haemophilus influenzae , reductase , enzyme , stereochemistry , biochemistry , amino acid , organic chemistry , antibiotics
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 P 4 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.