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Title: Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri

Abstract

The molybdate-binding protein (ModA) from X. axonopodis pv. citri was crystallized with sodium molybdate in the presence of PEG or sulfate. The crystal diffracted to a maximum resolution of 1.7 Å and belongs to the orthorhombic space group C222{sub 1,} with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å. Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 Å using synchrotron radiation. The crystal belongs to the orthorhombic space group C222{sub 1}, with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.

Authors:
; ;  [1];  [2];  [3]
  1. Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP (Brazil)
  2. Centro de Biologia Molecular e Estrutural (CeBiMe), Laboratório Nacional de Luz Síncrotron (LNLS), CP 6192, Campinas, SP 13084-971 (Brazil)
  3. (Brazil)
Publication Date:
OSTI Identifier:
22356297
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 3; Other Information: PMCID: PMC2197186; PMID: 16511325; PUBLISHER-ID: ll5045; OAI: oai:pubmedcentral.nih.gov:2197186; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CAPTURE; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; DIFFUSION; MOLYBDATES; PROTEINS; RESOLUTION; SODIUM; SPACE GROUPS; SULFATES; SYNCHROTRON RADIATION; X-RAY DIFFRACTION

Citation Formats

Santacruz, C. P., Balan, A., Ferreira, L. C. S., Barbosa, J. A. R. G., E-mail: joao@lnls.br, and Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP. Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106003812.
Santacruz, C. P., Balan, A., Ferreira, L. C. S., Barbosa, J. A. R. G., E-mail: joao@lnls.br, & Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP. Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. United Kingdom. doi:10.1107/S1744309106003812.
Santacruz, C. P., Balan, A., Ferreira, L. C. S., Barbosa, J. A. R. G., E-mail: joao@lnls.br, and Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP. 2006. "Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri". United Kingdom. doi:10.1107/S1744309106003812.
@article{osti_22356297,
title = {Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri},
author = {Santacruz, C. P. and Balan, A. and Ferreira, L. C. S. and Barbosa, J. A. R. G., E-mail: joao@lnls.br and Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP},
abstractNote = {The molybdate-binding protein (ModA) from X. axonopodis pv. citri was crystallized with sodium molybdate in the presence of PEG or sulfate. The crystal diffracted to a maximum resolution of 1.7 Å and belongs to the orthorhombic space group C222{sub 1,} with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å. Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 Å using synchrotron radiation. The crystal belongs to the orthorhombic space group C222{sub 1}, with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.},
doi = {10.1107/S1744309106003812},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 62,
place = {United Kingdom},
year = 2006,
month = 3
}
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