2GW2
Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-04-28 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.432, 65.504, 69.341 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.617 - 1.800 |
Rwork | 0.217 |
R-free | 0.27930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a58 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.474 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (refmac_5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 1.860 |
High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
Rmerge | 0.148 | 0.070 | 0.630 |
Number of reflections | 14841 | 1667 | 908 |
<I/σ(I)> | 5.8 | ||
Completeness [%] | 90.0 | ||
Redundancy | 4 | 4.4 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 2M ammonium sulfate, 0.2M sodium chloride, 0.1M HEPES, pH 7.5, vapor diffusion, sitting drop, temperature 291K |