Open AccessPurification, crystallization and preliminary crystallographic analysis of the CBS‐domain protein MJ1004 from Methanocaldococcus jannaschii
Author(s) -
Oyenarte Iker,
Lucas María,
Gómez García Inmaculada,
MartínezCruz Luis Alfonso
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110053479
Subject(s) - monoclinic crystal system , crystallography , crystallization , resolution (logic) , molecule , x ray crystallography , crystal structure , diffraction , domain (mathematical analysis) , chemistry , protein crystallization , synchrotron radiation , materials science , physics , optics , organic chemistry , mathematical analysis , mathematics , artificial intelligence , computer science
The purification and preliminary crystallographic analysis of the archaeal CBS‐domain protein MJ1004 from Methanocaldococcus jannaschii are described. The native protein was overexpressed, purified and crystallized in the monoclinic space group P 2 1 , with unit‐cell parameters a = 54.4, b = 53.8, c = 82.6 Å, β = 106.1°. The crystals diffracted X‐rays to 2.7 Å resolution using synchrotron radiation. Matthews‐volume calculations suggested the presence of two molecules in the asymmetric unit that are likely to correspond to a dimeric species, which is also observed in solution.