Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8. Issue 11 (1st November 2013)

• Record Type: Journal Article
• Authors: Wong, Jaslyn E. M. M.; Blaise, Mickael
• Is Part Of: Acta crystallographica. Volume 69:Issue 11(2013:Nov.)
• Page Start: 1291
• Page End: 1294
• Publication Date: 2013-11-01
• Subjects: peptidoglycan -- autolysin -- LysM -- NlpC/P60 -- endopeptidases -- TTHA0266 -- Thermus thermophilus; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113027164
• Languages: English
• ISSNs: 1744-3091

Abstract

Abstract : 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 overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution and belonged to the hexagonal space group P 61, with unit‐cell parameters a = b = 71.19, c = 198.68 Å, γ = 120°. Selenomethionine‐substituted protein was crystallized and the structure was solved by single‐wavelength anomalous dispersion.