Cloning, expression, purification, characterization, crystallization and x-ray diffraction of bifunctional pyrimidine deaminase/reductase from Shigella flexneri 2a.
Bifunctional pyrimidine deaminase/reductase (RibD) plays an important role during riboflavin biosynthesis in many microorganisms. The 40.4 kDa RibD from Shigella flexneri 2a has been cloned, expressed, purified and characterized. Three Crystals of RibD have been obtained by the hanging-drop technique at 291 K using PEG 20k or NaCl as precipitant. The RibD crystal using PEG 20k as precipitant diffracted to 2.5A.
College of Science, Beijing Forestry University, Beijing 100083, , China.
Daopeng
D
Yuan
Qihai
Q
Wang
Wei
W
Gao
Fanyi
F
Sheng
Zhanyu
Z
Zhang
Qingyu
Q
Lu
Huaixing
H
Cang
Ruchang
R
Bi
D000619:Aminohydrolases / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011743:Pyrimidines / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012763:Shigella flexneri / Q000201:enzymology* / Q000235:genetics
D011743:Pyrimidines; D011993:Recombinant Fusion Proteins; D010088:Oxidoreductases; D000619:Aminohydrolases; C030986:pyrimidine