
Crystallization and preliminary X‐ray analysis of the diadenosine 5′,5′′′‐ P 1 , P 4 ‐tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv
Author(s) -
Mori Shigetarou,
Shibayama Keigo,
Wachino Junichi,
Arakawa Yoshichika
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910905444x
Subject(s) - crystallization , mycobacterium tuberculosis , glycogen phosphorylase , nuclear chemistry , radiochemistry , physics , chemistry , tuberculosis , biochemistry , organic chemistry , enzyme , medicine , pathology
A novel diadenosine 5′,5′′′‐ P 1 , P 4 ‐tetraphosphate (Ap4A) phosphorylase (Rv2613c) from Mycobacterium tuberculosis H37Rv has been crystallized by the sitting‐drop vapour‐diffusion method. The crystal belonged to space group C 2, with unit‐cell parameters a = 101.5, b = 63.6, c = 79.1 Å, β = 110.9°. The diffraction of the crystals extended to 1.9 Å resolution. The asymmetric unit is expected to contain two molecules of Rv2613c, with a corresponding crystal volume per protein weight ( V M ) of 2.41 Å 3 Da −1 and a solvent content of 49.1%. This is the first report of a crystal of Ap4A phosphorylase.
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