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) |