CRYSTALLIZATION AND X-RAY-DIFFRACTION STUDY OF THE STREPTOMYCES K15 PENICILLIN-BINDING DD-TRANSPEPTIDASE

[摘要] The 262 amino acid residue long DD-transpeptidase/penicillin-binding protein of Streptomyces K15 has been crystallized at room temperature by using the hanging drop vapour diffusion technique. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 46.4 Angstrom, b = 54.1 Angstrom and c = 108.3 Angstrom. They contain one protein molecule per asymmetric unit and diffract to about 1.9 Angstrom. X-ray data have been collected to 2.0 Angstrom from a native crystal. The previously published amino acid sequence of the protein has been corrected at positions 71, 72, 113, 114 and 156.

[发布日期] 1994-08-12

[关键词] DD-TRANSPEPTIDASE;PENICILLIN-BINDING PROTEIN;MASS SPECTROMETRY;CRYSTALLIZATION;X-RAY ANALYSIS