Crystallization and structure determination of a symmetricalfootball'complex of the mammalian mitochondrial Hsp60–Hsp10 chaperonins
S Nisemblat, A Parnas, O Yaniv, A Azem… - … Section F: Structural …, 2014 - scripts.iucr.org
Acta Crystallographica Section F: Structural Biology Communications, 2014•scripts.iucr.org
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 …
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 …
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.
International Union of Crystallography