Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8

摘要

Autolysins belong to a protein family involved in peptidoglycan degradation and remodelling. Within this family, NlpC/P60 endopeptidases are involved in the hydrolysis of the peptide arm of peptidoglycan. In this work, the putative NlpC/P60 endopeptidase TTHA0266 from Thermus thermophilus HB8 was over-expressed, purified and crystallized. The crystals diffracted to 2.4 angstrom resolution and belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 71.19, c = 198.68 angstrom, gamma = 120 degrees. Selenomethionine-substituted protein was crystallized and the structure was solved by single-wavelength anomalous dispersion.