Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction

Journal Article · Tue Apr 01 00:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108004569· OSTI ID:22360515

Briers, Yves ^[1]; Derua, Rita; Waelkens, Etienne ^[2]; Lavigne, Rob ^[1]; Van Meervelt, Luc ^[3]

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1. Laboratory of Gene Technology, Biosystems Department, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, B-3001 Heverlee (Belgium)
2. Laboratory for Protein Phosphorylation and Proteomics and BioMacS, Molecular Cellbiology Department, Katholieke Universiteit Leuven, O&N I Herestraat 49, B-3000 Leuven (Belgium)
3. Biomolecular Architecture and BioMacS, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B-3001 Heverlee (Belgium)

Crystallization and X-ray data collection of the C-terminus of gp36 from bacteriophage ϕKMV (KMV36C) are reported. The C-terminus of gp36 of bacteriophage ϕKMV (KMV36C) functions as a particle-associated muramidase, presumably as part of the injection needle of the ϕKMV genome during infection. Crystals of KMV36C were obtained by hanging-drop vapour diffusion and diffracted to a resolution of 1.6 Å. The crystals belong to the cubic space group P432, with unit-cell parameters a = b = c = 102.52 Å. KMV36C shows 30% sequence identity to T4 lysozyme (PDB code)

• OSTI ID: 22360515
• Journal Information: Acta Crystallographica. Section F, Vol. 64, Issue Pt 4; Other Information: PMCID: PMC2374246; PMID: 18391422; PUBLISHER-ID: gj5037; OAI: oai:pubmedcentral.nih.gov:2374246; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
INJECTION
LYSOZYME
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION