Expression, purification, crystallization and preliminary X-ray analysis of a DNA-binding protein from Methanococcus jannaschii

• Published in: Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-07, Vol.58 (7), p.1240-1242
• Main Authors: Wang, Ganggang, Guo, Rong, Bartlam, Mark, Xue, Hong, Yang, Haitao, Liu, Yiwei, Huang, Li, Rao, Zihe
• Format: Article
• Language: English
• Subjects: Crystallography, X-Ray - methods; DNA-binding proteins; DNA-Binding Proteins - chemistry; Escherichia coli - metabolism; Methanococcus - chemistry; Plasmids - metabolism
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444902007679

A small DNA‐binding protein of 87 amino‐acid residues from the hyperthermophilic archaeon Methanococcus jannaschii (Mja10b) was cloned and overexpressed in Escherichia coli. The protein was crystallized and the crystals belong to the space group P6122/P6522, with unit‐cell parameters a = b = 50.85, c = 124.02 Å, α = β = 90, γ = 120°. The crystals diffracted to a maximum resolution of 2.2 Å at 100 K using Cu Kα radiation. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (VM) of 2.4 Å3 Da−1 and a solvent content of 49% by volume. A full set of X‐­ray diffraction data was collected to 2.2 Å from the native crystal.