Cloning, refolding, purification and preliminary crystallographic analysis of the sensory domain of the Campylobacter chemoreceptor for multiple ligands (CcmL)

Mayra A. Machuca, Yu C. Liu, Simone A. Beckham, Anna Roujeinikova

Research output: Contribution to journalArticleResearchpeer-review

Abstract

A periplasmic sensory domain of the Campylobacter jejuni chemoreceptor for multiple ligands (CcmL) has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 3350 as a precipitating agent. A complete data set was collected to 1.3 Å resolution using cryocooling conditions and synchrotron radiation. The crystals belonged to space group P21, with unit-cell parameters a = 42.6, b = 138.0, c = 49.0 Å, β = 94.3 º .
Original languageEnglish
Pages (from-to)211-216
Number of pages6
JournalActa Crystallographica. Section F: Structural Biology Communications
VolumeF71
Issue numberPart 2
DOIs
Publication statusPublished - 2015

Keywords

  • campylobacter jejuni
  • chemotaxis
  • transducer-like proteins
  • methyl-accepting proteins

Cite this

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title = "Cloning, refolding, purification and preliminary crystallographic analysis of the sensory domain of the Campylobacter chemoreceptor for multiple ligands (CcmL)",
abstract = "A periplasmic sensory domain of the Campylobacter jejuni chemoreceptor for multiple ligands (CcmL) has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 3350 as a precipitating agent. A complete data set was collected to 1.3 {\AA} resolution using cryocooling conditions and synchrotron radiation. The crystals belonged to space group P21, with unit-cell parameters a = 42.6, b = 138.0, c = 49.0 {\AA}, β = 94.3 º .",
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author = "Machuca, {Mayra A.} and Liu, {Yu C.} and Beckham, {Simone A.} and Anna Roujeinikova",
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doi = "10.1107/S2053230X1500045X",
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journal = "Acta Crystallographica. Section F: Structural Biology Communications",
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publisher = "International Union of Crystallography",
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}

Cloning, refolding, purification and preliminary crystallographic analysis of the sensory domain of the Campylobacter chemoreceptor for multiple ligands (CcmL). / Machuca, Mayra A.; Liu, Yu C.; Beckham, Simone A.; Roujeinikova, Anna.

In: Acta Crystallographica. Section F: Structural Biology Communications, Vol. F71, No. Part 2, 2015, p. 211-216.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Cloning, refolding, purification and preliminary crystallographic analysis of the sensory domain of the Campylobacter chemoreceptor for multiple ligands (CcmL)

AU - Machuca, Mayra A.

AU - Liu, Yu C.

AU - Beckham, Simone A.

AU - Roujeinikova, Anna

PY - 2015

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AB - A periplasmic sensory domain of the Campylobacter jejuni chemoreceptor for multiple ligands (CcmL) has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 3350 as a precipitating agent. A complete data set was collected to 1.3 Å resolution using cryocooling conditions and synchrotron radiation. The crystals belonged to space group P21, with unit-cell parameters a = 42.6, b = 138.0, c = 49.0 Å, β = 94.3 º .

KW - campylobacter jejuni

KW - chemotaxis

KW - transducer-like proteins

KW - methyl-accepting proteins

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JO - Acta Crystallographica. Section F: Structural Biology Communications

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