Literature DB >> 16511134

Cloning, purification crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC6422 from Xanthomonas campestris.

Chao-Yu Yang1, Ko-Hsin Chin, Chia-Cheng Chou, Hui-Lin Shr, Fei Philip Gao, Ping-Chiang Lyu, Andrew H-J Wang, Shan-Ho Chou.   

Abstract

Xanthomonas campestris pv. campestris is a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. Its genome contains approximately 4500 genes, roughly one third of which have no known structure and/or function. However, some genes of unknown function are highly conserved among several different bacterial genuses. XC6422 is one such conserved hypothetical protein and has been overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. Crystals grew to approximately 2 x 1.5 x 0.4 mm in size after one week and diffracted to at least 1.6 A resolution. They belong to the monoclinic space group C2, with one molecule per asymmetric unit and unit-cell parameters a = 75.8, b = 79.3, c = 38.2 A, beta = 109.4 degrees. Determination of this structure may provide insights into the protein's function.

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Year:  2005        PMID: 16511134      PMCID: PMC1952462          DOI: 10.1107/S1744309105019391

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  14 in total

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10.  Automated MAD and MIR structure solution.

Authors:  T C Terwilliger; J Berendzen
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  1 in total

1.  Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase.

Authors:  Chao Yu Yang; Ko Hsin Chin; Chia Cheng Chou; Andrew H J Wang; Shan Ho Chou
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-05-31
  1 in total

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