Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C: crystallization and preliminary X-ray diffraction.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 64(Pt 4): 263-5, 2008 Apr 01.
Article
en En
| MEDLINE
| ID: mdl-18391422
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).
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fagos Pseudomonas
/
N-Acetil Muramoil-L-Alanina Amidasa
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2008
Tipo del documento:
Article