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

Kristof Van Hecke UGent, Yves Briers UGent, Rita Derua, Etienne Waelkens, Rob Lavigne and Luc Van Meervelt (2008) ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. 64(4). p.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).
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PHI-KMV, PSEUDOMONAS-AERUGINOSA, LYSOZYME, STABILITY
journal title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Acta Crystallogr. F-Struct. Biol. Cryst. Commun.
volume
64
issue
4
pages
263 - 265
Web of Science type
Article
Web of Science id
000254473200009
JCR category
CRYSTALLOGRAPHY
JCR impact factor
0.606 (2008)
JCR rank
19/25 (2008)
JCR quartile
4 (2008)
ISSN
1744-3091
DOI
10.1107/S1744309108004569
language
English
UGent publication?
no
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2045738
handle
http://hdl.handle.net/1854/LU-2045738
date created
2012-02-27 11:02:18
date last changed
2018-06-29 11:47:22
@article{2045738,
  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).},
  author       = {Van Hecke, Kristof and Briers, Yves and Derua, Rita and Waelkens, Etienne and Lavigne, Rob and Van Meervelt, Luc},
  issn         = {1744-3091},
  journal      = {ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS},
  keyword      = {PHI-KMV,PSEUDOMONAS-AERUGINOSA,LYSOZYME,STABILITY},
  language     = {eng},
  number       = {4},
  pages        = {263--265},
  title        = {Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C : crystallization and preliminary X-ray diffraction},
  url          = {http://dx.doi.org/10.1107/S1744309108004569},
  volume       = {64},
  year         = {2008},
}

Chicago
Van Hecke, Kristof, Yves Briers, Rita Derua, Etienne Waelkens, Rob Lavigne, and Luc Van Meervelt. 2008. “Structural Analysis of Bacteriophage-encoded Peptidoglycan Hydrolase Domain KMV36C : Crystallization and Preliminary X-ray Diffraction.” Acta Crystallographica Section F-structural Biology and Crystallization Communications 64 (4): 263–265.
APA
Van Hecke, K., Briers, Y., Derua, R., Waelkens, E., Lavigne, R., & Van Meervelt, L. (2008). Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C : crystallization and preliminary X-ray diffraction. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 64(4), 263–265.
Vancouver
1.
Van Hecke K, Briers Y, Derua R, Waelkens E, Lavigne R, Van Meervelt L. Structural analysis of bacteriophage-encoded peptidoglycan hydrolase domain KMV36C : crystallization and preliminary X-ray diffraction. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. 2008;64(4):263–5.
MLA
Van Hecke, Kristof, Yves Briers, Rita Derua, et al. “Structural Analysis of Bacteriophage-encoded Peptidoglycan Hydrolase Domain KMV36C : Crystallization and Preliminary X-ray Diffraction.” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 64.4 (2008): 263–265. Print.