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Crystallization of the cpn6O/cpn10 complex (‘holo‐chaperonin’) from Thermus thermophilus
Author(s) -
Lissin N.M.,
Sedelnikova S.E.,
Ryazantsev S.N.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81357-r
Subject(s) - chaperonin , thermus thermophilus , groel , groes , thermophile , thermus , crystallization , crystallography , escherichia coli , materials science , chemistry , bacteria , biology , protein folding , biochemistry , organic chemistry , paleontology , gene
A stable complex of the chaperonins, cpn60 and cpn10 ( Escherichia coli GroEL and GroES homologues), from the extremely thermophilic bacterium Thermus thermophilis has been isolated and crystallized. The crystals have dimensions up to 30 × 200 × 200 μm. 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, γ=90°.