Open AccessIsolation, crystallization and preliminary X‐ray analysis of a methanol‐induced corrinoid protein from Moorella thermoacetica
Author(s) -
Zhou Weihong,
Das Amaresh,
Liu ZhiJie,
Chen Lirong,
Chang Jessie,
Lee Doowon,
Habel Jeff E.,
Nguyen Duong,
Tempel Wolfram,
Rose John P.,
Chang ShuHuey,
Ljungdahl Lars G.,
Wang BiCheng
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105010511
Subject(s) - corrinoid , orthorhombic crystal system , crystallization , crystallography , methanol , chemistry , monoclinic crystal system , thermophile , biochemistry , enzyme , crystal structure , methyltransferase , gene , organic chemistry , methylation
A corrinoid protein was induced and overexpressed in methanol‐grown cells of the thermophilic anaerobic bacterium Moorella thermoacetica . The protein was purified from cytosolic extracts. After screening for crystallization conditions and optimization, crystals were obtained that diffracted strongly on a rotating‐anode X‐ray source. A diffraction data set was collected and processed including reflections to 1.9 Å resolution. Reflections were indexed in a primitive orthorhombic cell with unit‐cell parameters a = 55.69, b = 62.74, c = 34.54 Å. N‐terminal amino‐acid sequencing indicates that the crystals contain a C‐terminal fragment of the protein.