Protein Preparation, Crystallization and Preliminary X-ray Crystallographic Analysis of Smu_195c From Caries Pathogen Streptococcus mutans
- VernacularTitle:龋齿致病菌变性链球菌蛋白Smu_195c的制备、结晶及初级晶体学分析
- Author:
Zengqiang GAO
;
Haifeng HOU
;
Liqin LI
;
Rui XU
;
Yuhe LIANG
;
Lanfen LI
;
Xiaodong SU
;
Yuhui DONG
- Publication Type:Journal Article
- Keywords:
Streptococcus mutans;
Smu_195c;
crystallization;
X-ray diffraction
- From:
Progress in Biochemistry and Biophysics
2007;34(2):203-206
- CountryChina
- Language:Chinese
-
Abstract:
Smu_195c is a protein with 86 amino acids in Streptococcus mutans, a primary pathogen for human dental caries. The specific function of Smu_195c is still unknown and there are no conserved domains in it. In order to find out its function, the gene encodes Smu_195c was cloned and expressed in E. coli as N-terminally 6*His tagged recombinant protein. Two crystal forms were obtained by the hanging drop method. Form Ⅰ belongs to space group P6122 or P6522 with the unit cell parameters a = b = 62.93 (A), c= 90.63 (A), γ=120° and form Ⅱ belongs to the space group P41212 or P43212 with the unit cell parameters a =b=57.97 (A), c = 103.51 (A).Crystals from the protein with His-tag belong to form Ⅰ, however, crystals from the protein without His-tag belong to both.
