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Title: Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu

Abstract

Bacteriophage Mu baseplate protein gene product 44 was crystallized. The crystal belongs to space group R3, with unit-cell parameters a = b = 126.6, c = 64.2 Å. Bacteriophage Mu baseplate protein gene product 44 (gp44) is an essential protein required for the assembly of viable phages. To investigate the roles of gp44 in baseplate assembly and infection, gp44 was crystallized at pH 6.0 in the presence of 20% 2-methyl-2,4-pentanediol. The crystals belong to space group R3, with unit-cell parameters a = b = 127.47, c = 63.97 Å. The crystals diffract X-rays to at least 2.1 Å resolution and are stable in the X-ray beam and are therefore appropriate for structure determination. Native data have been collected to 2.1 Å resolution using a DIP6040 image-plate system at beamline BL44XU at the SPring-8 facility in Japan.

Authors:
 [1]; ;  [2];  [1]; ;  [3];  [1]
  1. Institute for Protein Research, Osaka University, Yamada-oka, Suita 565-0871 (Japan)
  2. Department of Nano-Material Systems Graduate School of Engineering, Gunma University, 1-5-1 Tenjin-chyo, Kiryu, Gunma 376-8515 (Japan)
  3. Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama (Japan)
Publication Date:
OSTI Identifier:
22356090
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 1; Other Information: PMCID: PMC1952399; PMID: 16508104; PUBLISHER-ID: en5076; OAI: oai:pubmedcentral.nih.gov:1952399; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BEAMS; CRYSTALLIZATION; CRYSTALS; IMAGES; PLATES; PROTEINS; RESOLUTION; SPACE GROUPS

Citation Formats

Kondou, Youhei, Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama, Kitazawa, Daisuke, Takeda, Shigeki, Yamashita, Eiki, Mizuguchi, Mineyuki, Kawano, Keiichi, and Tsukihara, Tomitake. Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309104029574.
Kondou, Youhei, Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama, Kitazawa, Daisuke, Takeda, Shigeki, Yamashita, Eiki, Mizuguchi, Mineyuki, Kawano, Keiichi, & Tsukihara, Tomitake. Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu. United Kingdom. https://doi.org/10.1107/S1744309104029574
Kondou, Youhei, Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama, Kitazawa, Daisuke, Takeda, Shigeki, Yamashita, Eiki, Mizuguchi, Mineyuki, Kawano, Keiichi, and Tsukihara, Tomitake. 2005. "Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu". United Kingdom. https://doi.org/10.1107/S1744309104029574.
@article{osti_22356090,
title = {Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu},
author = {Kondou, Youhei and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama and Kitazawa, Daisuke and Takeda, Shigeki and Yamashita, Eiki and Mizuguchi, Mineyuki and Kawano, Keiichi and Tsukihara, Tomitake},
abstractNote = {Bacteriophage Mu baseplate protein gene product 44 was crystallized. The crystal belongs to space group R3, with unit-cell parameters a = b = 126.6, c = 64.2 Å. Bacteriophage Mu baseplate protein gene product 44 (gp44) is an essential protein required for the assembly of viable phages. To investigate the roles of gp44 in baseplate assembly and infection, gp44 was crystallized at pH 6.0 in the presence of 20% 2-methyl-2,4-pentanediol. The crystals belong to space group R3, with unit-cell parameters a = b = 127.47, c = 63.97 Å. The crystals diffract X-rays to at least 2.1 Å resolution and are stable in the X-ray beam and are therefore appropriate for structure determination. Native data have been collected to 2.1 Å resolution using a DIP6040 image-plate system at beamline BL44XU at the SPring-8 facility in Japan.},
doi = {10.1107/S1744309104029574},
url = {https://www.osti.gov/biblio/22356090}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 1,
volume = 61,
place = {United Kingdom},
year = {Sat Jan 01 00:00:00 EST 2005},
month = {Sat Jan 01 00:00:00 EST 2005}
}