Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 70, Issue -, Pages 116-119Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X1303389X
Keywords
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Funding
- Morasha program of the Israel Science Foundation [1902/08]
- Israel Science Foundation [452/09]
- Eshkol Fellowship from the Ministry of Science
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The mitochondrial Hsp60-Hsp10 complex assists the folding of various proteins impelled by ATP hydrolysis, similar to the bacterial chaperonins GroEL and GroES. The near-atomic structural details of the mitochondrial chaperonins are not known, despite the fact that almost two decades have passed since the structures of the bacterial chaperonins became available. Here, the crystallization procedure, diffraction experiments and structure determination by molecular replacement of the mammalian mitochondrial chaperonin HSP60 (E321K mutant) and its co-chaperonin Hsp10 are reported.
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