Crystallization and preliminary X-ray crystallographic analysis of the tRNA-specific adenosine deaminase from Streptococcus pyogenes.
The tRNA-specific adenosine deaminase from the pathogenic bacteria Streptococcus pyogenes (spTAD) has been overexpressed in Escherichia coli and crystallized in the presence of Zn2+ ion at 295 K using ammonium sulfate as a precipitant. Flash-cooled crystals of spTAD diffracted to 2.0 A using 30%(v/v) glycerol as a cryoprotectant. X-ray diffraction data have been collected to 2.0 A using synchrotron radiation. The crystal belongs to the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 81.042, c = 81.270 A. The asymmetric unit contains one subunit of spTAD, with a corresponding crystal volume per protein weight (VM) of 3.3 A3 Da(-1) and a solvent content of 62.7%.
Ku
Min-Je
MJ
Functional Proteomics Center, Korea Institute of Science and Technology, 39-1 Hawolgok-dong, Seongbuk-gu, Seoul 136-791, South Korea.
Lee
Won-Ho
WH
Nam
Ki-hyun
KH
Rhee
Kyeong-hee
KH
Lee
Ki-Seog
KS
Kim
Eunice EunKyung
EE
Yu
Myung-Hee
MH
Hwang
Kwang Yeon
KY
D000243:Adenosine Deaminase / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D011232:Chemical Precipitation; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D016601:RNA-Binding Proteins; D013297:Streptococcus pyogenes / Q000201:enzymology*
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase