Crystallization and preliminary crystallographic analysis of merohedrally twinned crystals of MJ0729, a CBS-domain protein from Methanococcus jannaschii.
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.
Fernández-Millán
Pablo
P
Unidad de Cristalografía Macromolecular, CIC bioGUNE, Parque Tecnológico de Vizcaya, Ed. 800, 48160 Derio, Vizcaya, Spain.
Kortazar
Danel
D
Lucas
María
M
Martínez-Chantar
María Luz
ML
Astigarraga
Egoitz
E
Fernández
José Andrés
JA
Sabas
Olatz
O
Albert
Armando
A
Mato
Jose M
JM
Martínez-Cruz
Luis Alfonso
LA
D020816:Amino Acid Motifs; D019843:Archaeal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D003541:Cystathionine beta-Synthase / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D017017:Methanococcus / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D013237:Stereoisomerism
D019843:Archaeal Proteins; D003541:Cystathionine beta-Synthase