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

JOURNAL OF MOLECULAR BIOLOGY

卷:241

Note

ENGLEBERT, S ; CHARLIER, P ; FONZE, E ; TOTH, Y ; VERMEIRE, M ; VANBEEUMEN, J ; GRANDCHAMPS, J ; HOFFMANN, K ; LEYHBOUILLE, M ; NGUYENDISTECHE, M ; GHUYSEN, JM

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

DOI  :  10.1006/jmbi.1994.1504

来源: Elsevier

【 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.

【 授权许可】

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