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Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):970-5. doi: 10.1107/S2053230X14010449. Epub 2014 Jun 19.

Crystallization of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34.

Author information

1
Departamento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), Calle Darwin 3, 28046 Madrid, Spain.
2
Department of Biological Sciences, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, B-9 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
3
Unit for Virus Host-Cell Interactions, Université Grenoble Alpes-EMBL-CNRS, 6 Rue Jules Horowitz, 38042 Grenoble, France.

Abstract

The phage-proximal part of the long tail fibres of bacteriophage T4 consists of a trimer of the 1289 amino-acid gene product 34 (gp34). Different carboxy-terminal parts of gp34 have been produced and crystallized. Crystals of gp34(726-1289) diffracting X-rays to 2.9 Å resolution, crystals of gp34(781-1289) diffracting to 1.9 Å resolution and crystals of gp34(894-1289) diffracting to 3.0 and 2.0 Å resolution and belonging to different crystal forms were obtained. Native data were collected for gp34(726-1289) and gp34(894-1289), while single-wavelength anomalous diffraction data were collected for selenomethionine-containing gp34(781-1289) and gp34(894-1289). For the latter, high-quality anomalous signal was obtained.

KEYWORDS:

bacteriophage T4; gene product 34 (gp34)

PMID:
25005101
PMCID:
PMC4089544
DOI:
10.1107/S2053230X14010449
[Indexed for MEDLINE]
Free PMC Article

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