Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the CBS‐domain pair from the Methanococcus jannaschii protein MJ0100
Author(s) -
Lucas María,
Kortazar Danel,
Astigarraga Egoitz,
Fernández José A.,
Mato Jose M.,
MartínezChantar María Luz,
MartínezCruz Luis Alfonso
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108027930
Subject(s) - methanococcus , orthorhombic crystal system , crystallography , crystallization , sequence (biology) , x ray crystallography , protein crystallization , protein domain , chemistry , biology , stereochemistry , crystal structure , materials science , biochemistry , diffraction , gene , escherichia coli , physics , organic chemistry , optics
CBS domains are small protein motifs consisting of a three‐stranded β‐sheet and two α‐helices that are present in proteins of all kingdoms of life and in proteins with completely different functions. Several genetic diseases in humans have been associated with mutations in their sequence, which has made them promising targets for rational drug design. The C‐terminal domain of the Methanococcus jannaschii protein MJ0100 includes a CBS‐domain pair and has been overexpressed, purified and crystallized. Crystals of selenomethionine‐substituted (SeMet) protein were also grown. The space group of both the native and SeMet crystals was determined to be orthorhombic P 2 1 2 1 2 1 , with unit‐cell parameters a = 80.9, b = 119.5, c = 173.3 Å. Preliminary analysis of the X‐ray data indicated that there were eight molecules per asymmetric unit in both cases.