Title: Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: Crystallization and preliminary X-ray diffraction
Authors: Van Hecke, Kristof * ×
Briers, Yves *
Derua, Rita
Waelkens, Etienne
Lavigne, Rob
Van Meervelt, Luc #
Issue Date: Apr-2008
Publisher: Wiley-blackwell publishing, inc
Series Title: Acta Crystallographica F, Structural Biology and Crystallization Communications Online vol:64 pages:263-265
Abstract: The C-terminus of gp36 of bacteriophage phi KMV ( KMV36C) functions as a particle-associated muramidase, presumably as part of the injection needle of the phi KMV genome during infection. Crystals of KMV36C were obtained by hanging-drop vapour diffusion and diffracted to a resolution of 1.6 angstrom. The crystals belong to the cubic space group P432, with unit-cell parameters a = b = c = 102.52 angstrom. KMV36C shows 30% sequence identity to T4 lysozyme ( PDB code 1156).
ISSN: 1744-3091
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Division of Gene Technology (-)
Molecular Imaging and Photonics
Biochemistry Section (Medicine) (-)
Biochemistry, Molecular and Structural Biology Section
Laboratory of Protein Phosphorylation and Proteomics
Laboratory of Phosphoproteomics (-)
* (joint) first author
× corresponding author
# (joint) last author

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