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Cloning, expression, and crystallization of Cpn60 proteins from Thermococcus litoralis
- Source :
- Scopus-Elsevier
- Publication Year :
- 2000
- Publisher :
- Polskie Towarzystwo Biochemiczne (Polish Biochemical Society), 2000.
-
Abstract
- Two genes of the extreme thermophilic archaeon Thermococcus litoralis homologous to those that code for Cpn60 chaperonins were cloned and expressed in Escherichia coli. Each of the Cpn60 subunits as well as the entire Cpn60 complex crystallize in a variety of morphological forms. The best crystals diffract to 3.6 A resolution at room temperature and belong to the space group 1422 with unit cell parameters a = b = 193.5 A, c = 204.2 A.
- Subjects :
- Cloning
Chaperonins
Protein Conformation
Thermophile
Biology
medicine.disease_cause
biology.organism_classification
General Biochemistry, Genetics and Molecular Biology
Chaperonin
Thermococcus
enzymes and coenzymes (carbohydrates)
Biochemistry
Heat shock protein
medicine
bacteria
Electrophoresis, Polyacrylamide Gel
Cloning, Molecular
Crystallization
Thermococcus litoralis
Escherichia coli
Gene
Archaea
Subjects
Details
- ISSN :
- 1734154X and 0001527X
- Volume :
- 47
- Database :
- OpenAIRE
- Journal :
- Acta Biochimica Polonica
- Accession number :
- edsair.doi.dedup.....2b6e779c68bc1b2d8ee64aafb4d50c14
- Full Text :
- https://doi.org/10.18388/abp.2000_4079