1ZKC
Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-04-16 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 65.028, 65.028, 201.790 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.970 - 1.650 |
R-factor | 0.15775 |
Rwork | 0.156 |
R-free | 0.19376 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iip |
RMSD bond length | 0.013 |
RMSD bond angle | 1.333 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.055 | 0.479 |
Number of reflections | 57395 | |
<I/σ(I)> | 31.86 | 1.72 |
Completeness [%] | 94.4 | 63.2 |
Redundancy | 5.6 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 298 | 0.8M Potassium Sodium Tartrate tetrahydrate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K, pH 7.50 |