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 |
