Ku, MJ Lee, WH Nam, KH Rhee, KH Lee, KS Kim, EE Yu, MH Hwang, KY 2024-01-21T05:11:25Z 2024-01-21T05:11:25Z 2021-09-03 2005-04 2053-230X https://pubs.kist.re.kr/handle/201004/136607 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 angstrom 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 angstrom. The asymmetric unit contains one subunit of spTAD, with a corresponding crystal volume per protein weight (V-M) of 3.3 angstrom(3) Da(-1) and a solvent content of 62.7%. English INT UNION CRYSTALLOGRAPHY COMPLETE GENOME SEQUENCE ESCHERICHIA-COLI STRAIN Crystallization and preliminary X-ray crystallographic analysis of the tRNA-specific adenosine deaminase from Streptococcus pyogenes Article 10.1107/S1744309105007311 1 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.61, pp.375 - 377 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 61 375 377 scie scopus 000232293200011 2-s2.0-33744499464 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article COMPLETE GENOME SEQUENCE ESCHERICHIA-COLI STRAIN