Open AccessCrystallization and preliminary crystallographic analysis of merohedrally twinned crystals of MJ0729, a CBS‐domain protein from Methanococcus jannaschii
Author(s) -
FernándezMillán Pablo,
Kortazar Danel,
Lucas María,
MartínezChantar María Luz,
Astigarraga Egoitz,
Fernández José Andrés,
Sabas Olatz,
Albert Armando,
Mato Jose M.,
MartínezCruz Luis Alfonso
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108013432
Subject(s) - crystal twinning , methanococcus , crystallography , crystallization , materials science , trigonal crystal system , chemistry , crystal structure , gene , biochemistry , microstructure , organic chemistry , escherichia coli
CBS domains are small protein motifs, usually associated in tandem, that are implicated in binding to adenosyl groups. Several genetic diseases in humans have been associated with mutations in CBS sequences, which has made them very promising targets for rational drug design. Trigonal crystals of the CBS‐domain protein MJ0729 from Methanococcus jannaschii were grown by the vapour‐diffusion method at acidic pH. Preliminary analysis of nine X‐ray diffraction data sets using Yeates statistics and Britton plots showed that slight variation in the pH as well as in the buffer used in the crystallization experiments led to crystals with different degrees of merohedral twinning that may vary from perfect hemihedral twinning to perfect tetartohedral twinning.