title: Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction.
abstract: The C-terminus of gp36 of bacteriophage varphiKMV (KMV36C) functions as a particle-associated muramidase, presumably as part of the injection needle of the phiKMV genome during infection. Crystals of KMV36C were obtained by hanging-drop vapour diffusion and diffracted to a resolution of 1.6 A. The crystals belong to the cubic space group P432, with unit-cell parameters a = b = c = 102.52 A. KMV36C shows 30% sequence identity to T4 lysozyme (PDB code 1l56).
authors.affiliation: Biomolecular Architecture and BioMacS, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200F, B-3001 Heverlee, Belgium. kristof.vanhecke@chem.kuleuven.be <kristof.vanhecke@chem.kuleuven.be>
authors.forename: Kristof
authors.initials: K
authors.lastname: Van Hecke
authors.forename: Yves
authors.initials: Y
authors.lastname: Briers
authors.forename: Rita
authors.initials: R
authors.lastname: Derua
authors.forename: Etienne
authors.initials: E
authors.lastname: Waelkens
authors.forename: Rob
authors.initials: R
authors.lastname: Lavigne
authors.forename: Luc
authors.initials: L
authors.lastname: Van Meervelt
mesh_terms: D003460:Crystallization; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000032:analysis / Q000737:chemistry*; D017902:Podoviridae / Q000737:chemistry / Q000201:enzymology; D017434:Protein Structure, Tertiary; D017105:Pseudomonas Phages / Q000737:chemistry* / Q000201:enzymology; D014961:X-Ray Diffraction
chemical_list: D009238:N-Acetylmuramoyl-L-alanine Amidase