Open AccessCloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor‐dependent phosphoglycerate mutase from Mycobacterium tuberculosis
Author(s) -
Watkins Harriet A.,
Yu MinMin,
Baker Edward N.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105020646
Subject(s) - mutase , phosphoglycerate mutase , mycobacterium tuberculosis , cofactor , cloning (programming) , mycobacterium , crystallography , chemistry , biology , tuberculosis , biochemistry , genetics , enzyme , bacteria , glycolysis , medicine , computer science , programming language , pathology
The Mycobacterium tuberculosis open reading frame Rv3214, annotated as a cofactor‐dependent phosphoglycerate mutase, has been cloned and expressed as an N‐terminally His‐tagged protein. Tagged, untagged and selenomethionine‐labelled forms of Rv3214 (EntD) have been purified using nickel‐affinity chromatography and gel filtration. The selenomethionine‐labelled crystals diffracted to 2.15 Å resolution and belong to space group P 2 1 , with unit‐cell parameters a = 44.36, b = 79.03, c = 52.85 Å, β = 109.11°. There are two molecules of molecular weight 21 948 Da per asymmetric unit.