Expression, Purification, Crystallization and Preliminary X-ray Studies of a Deoxycytidylate Deaminase From Streptococcus mutans
- VernacularTitle:来自于变性链球菌的脱氧胞嘧啶核苷酸脱氨酶的表达,纯化,结晶以及初步晶体学研究
- Author:
Haifeng HOU
;
Zengqiang GAO
;
Jianhua XU
;
Rui XU
;
Liqin LI
;
Lanfen LI
;
Yuhe LIANG
;
Xiaodong SU
;
Peng LIU
;
Dingchang XIAN
;
Yuhui DONG
- Publication Type:Journal Article
- Keywords:
deoxycytidylate deaminase;
Streptococcus mutans;
allosteric regulation;
crystallization
- From:
Progress in Biochemistry and Biophysics
2006;33(7):673-676
- CountryChina
- Language:Chinese
-
Abstract:
Deoxycytidylate (dCMP) deaminase is an enzyme belonged to dCMP cyt deam family. The dCMP deaminase from Streptococcus mutans UA159 was cloned and expressed in E. coli, and purified to homogeneity. The FPLC size exclusion chromatography analysis reveals that the S. mutans dCMP deaminase forms hexamer in solution. The protein was crystallized using hanging drop vapour-diffusion method and diffracted to a resolution of 3.1 (A). The diffraction data were collected at BSRF beamline3W1A. The crystals belong to P213 space group, with unit cell parameters a = b = c = 113.2(A), α =β = γ = 90°. Assuming there are two subunits per asymmetric unit, the Matthews coefficient is 3.6 (A)3 ·Da-1. This is the first crystallization report of the wild-type deoxycytidylate deaminase.
