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PMID: 1356830 Published · ppublish English Journal Article

Crystallization of the cpn60/cpn10 complex ('holo-chaperonin') from Thermus thermophilus.

FEBS letters ·Vol. 311 ·No. 1 ·1992-10-12 ·Pages 22-4

Lissin NM, Sedelnikova SE, Ryazantsev SN

Abstract

A stable complex of the chaperonins, cpn60 and cpn10 (Escherichia coli GroEL and GroES homologues), from the extremely thermophilic bacterium Thermus thermophilus has been isolated and crystallized. The crystals have dimensions up to 30 x 200 x 200 microns. Ultra-thin sections of the crystals estimated by electron microscopy showed a rectangular lattice with unit cell parameters of a = 17 nm, b = 27 nm, gamma = 90 degrees.

MeSH Terms
Bacterial Proteins/isolation & purification,ultrastructure Chaperonin 10 Chaperonin 60 Chaperonins Crystallization Heat-Shock Proteins/isolation & purification,ultrastructure Macromolecular Substances Proteins/isolation & purification,ultrastructure Thermus thermophilus/chemistry
Chemicals
Bacterial Proteins Chaperonin 10 Chaperonin 60 Heat-Shock Proteins Macromolecular Substances Proteins Chaperonins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lissin N M
Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.
Sedelnikova S E
Ryazantsev S N
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1992-10-12
Pages
22-4
Language
English
Region
England
NLM ID
0155157
Subset
IM
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