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

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 condit...

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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2015-02, Vol.71 (2), p.211-216
Main Authors: Machuca, Mayra A., Liu, Yu C., Beckham, Simone A., Roujeinikova, Anna
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Campylobacter - chemistry
Campylobacter jejuni
chemotaxis
Chromatography, Gel
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Electrophoresis, Polyacrylamide Gel
Ligands
Light
methyl-accepting proteins
Molecular Sequence Data
Protein Refolding
Protein Structure, Tertiary
Research Communications
Scattering, Radiation
transducer-like proteins
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Summary: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°.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X1500045X