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

Van Hecke Kristof | Zendy; Briers Yves | Zendy; Derua Rita | Zendy; Waelkens Etienne | Zendy; Lavigne Rob | Zendy; Van Meervelt Luc | Zendy

Open Access

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

Author(s) -

Van Hecke Kristof,

Briers Yves,

Derua Rita,

Waelkens Etienne,

Lavigne Rob,

Van Meervelt Luc

Publication year - 2008

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309108004569

Subject(s) - crystallography , bacteriophage , lysozyme , crystallization , peptidoglycan , diffraction , resolution (logic) , protein data bank (rcsb pdb) , materials science , chemistry , optics , biochemistry , physics , enzyme , escherichia coli , gene , organic chemistry , artificial intelligence , computer science

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 P 432, with unit‐cell parameters a = b = c = 102.52 Å. KMV36C shows 30% sequence identity to T4 lysozyme (PDB code 1l56 ).

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