4PJ1

Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2013-12-12
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.95370
Spacegroup name	P 41 21 2
Unit cell lengths	199.100, 199.100, 627.390
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.775 - 3.150
R-factor	0.2422
Rwork	0.241
R-free	0.27040
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1aon
RMSD bond length	0.004
RMSD bond angle	1.109
Data reduction software	XDS (0.2.14)
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.780	49.780	3.260
High resolution limit [Å]	3.150	12.200	3.150
Rmerge	0.136	0.034	1.491
Rpim	0.058	0.015	0.793
Total number of observations	1351770	24461	85114
Number of reflections	217130
<I/σ(I)>	9	30.6	0.7
Completeness [%]	99.8	98.5	99.1
Redundancy	6.2	5.9	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		303	Protein concentration: mHsp60, 9.5 mg/ml ; mHsp10, 1.6 mg/ml; Composition of protein solution: 50 mM Tris-HCl pH 7.7, 300 mM NaCl, 5% glycerol, 15 mM MgCl2, 0.5 mM KCl,1 mM ATP; Composition of reservoir solution: 0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dehydrate,30-35%(v/v) PEG 400 Volume and ratio of drop:5 micro l (1:1)