Subcloning of a dna fragment encoding a single cohesin domain of the clostridium thermocellum cellulosome‐integrating protein cipA: Purification, crystallization, and preliminary diffraction analysis of the encoded polypeptide

An Escherichia coli clone encoding a single cohesin domain of the cellulosome‐integrating protein CipA from Clostridium thermocellum was constructed, and the corresponding polypeptide was purified, treated with papain, and crystallized from a PEG 8000 solution. Crystals exhibit orthorhombic symmetry...

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Bibliographic Details
Published in:Protein science 1996-06, Vol.5 (6), p.1192-1194
Main Authors: Béguin, Pierre, Raynaud, Odette, Chaveroche, Marie‐Kim, Dridi, Abel, Alzari, Pedro M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Base Sequence
Biochemistry, Molecular Biology
Bioinformatics
Biological Physics
Carrier Proteins
Carrier Proteins - genetics
Cellular Biology
Chemical Sciences
Cloning, Molecular
Clostridium
Clostridium - chemistry
Clostridium - genetics
Clostridium thermocellum
cohesin domain
Computer Science
Cristallography
Crystallization
Crystallography, X-Ray
DNA, Bacterial
DNA, Bacterial - genetics
DNA, Recombinant
DNA, Recombinant - genetics
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Escherichia coli - genetics
Gene Expression
Life Sciences
Membrane Proteins
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - isolation & purification
Physics
Plasmids
Recombinant Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
scaffolding protein
Structural Biology
X‐ray crystallography
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Description
Summary:An Escherichia coli clone encoding a single cohesin domain of the cellulosome‐integrating protein CipA from Clostridium thermocellum was constructed, and the corresponding polypeptide was purified, treated with papain, and crystallized from a PEG 8000 solution. Crystals exhibit orthorhombic symmetry, space group P212121, with cell dimensions a = 37.7 Å, b = 80.7 Å, c = 93.3 Å, and four or eight molecules in the unit cell. The crystals diffract X‐rays to beyond 2 Å resolution and are suitable for further crystallographic studies.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560050623