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

doi:10.1107/S2053230X1500045X

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 journal › Article › Research › peer-review

7 Citations (Scopus)

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 language	English
Pages (from-to)	211-216
Number of pages	6
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	F71
Issue number	Part 2
DOIs	https://doi.org/10.1107/S2053230X1500045X
Publication status	Published - 2015

Keywords

campylobacter jejuni
chemotaxis
transducer-like proteins
methyl-accepting proteins

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10.1107/S2053230X1500045X

Cite this

@article{308a7e90aa514bbfac92dd3661ce1f73,

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 .",

keywords = "campylobacter jejuni, chemotaxis, transducer-like proteins, methyl-accepting proteins",

author = "Machuca, \{Mayra A.\} and Liu, \{Yu C.\} and Beckham, \{Simone A.\} and Anna Roujeinikova",

year = "2015",

doi = "10.1107/S2053230X1500045X",

language = "English",

volume = "F71",

pages = "211--216",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

issn = "1744-3091",

publisher = "International Union of Crystallography (IUCr)",

number = "Part 2",

}

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

Research output: Contribution to journal › Article › Research › peer-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

Y1 - 2015

N2 - 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 .

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

UR - http://journals.iucr.org/f/issues/2015/02/00/wd5241/wd5241.pdf

UR - https://www.scopus.com/pages/publications/84922744202

U2 - 10.1107/S2053230X1500045X

DO - 10.1107/S2053230X1500045X

M3 - Article

SN - 1744-3091

VL - F71

SP - 211

EP - 216

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Part 2

ER -

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

Abstract

Keywords

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Understanding the molecular mechanism of force generation in the bacterial flagellar motor

Monash Macromolecular Crystallisation Platform (MMCP)

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

Abstract

Keywords

Access to Document

Other files and links

Projects

Understanding the molecular mechanism of force generation in the bacterial flagellar motor

Equipment

Monash Macromolecular Crystallisation Platform (MMCP)

Cite this