4OAQ
Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 93 |
Detector technology | IMAGE PLATE |
Collection date | 2012-09-19 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.724, 99.896, 116.662 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.974 - 1.858 |
R-factor | 0.2038 |
Rwork | 0.201 |
R-free | 0.24950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1piw |
RMSD bond length | 0.008 |
RMSD bond angle | 1.225 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.974 | 1.930 |
High resolution limit [Å] | 1.858 | 1.860 |
Rmerge | 0.089 | 0.590 |
Number of reflections | 62705 | |
<I/σ(I)> | 5.46 | 2.13 |
Completeness [%] | 96.1 | 97.7 |
Redundancy | 4.9 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | protein sample (13.5 mg/ml) was mixed with an equal volume of reservoir solution and equilibrated against the latter. The reservoir solution consisted of 25%(w/v) PEG 4000 as a precipitant, 0.1 M HEPES pH 7.5 as buffer, and 8% isopropanol and 0.1 mM ZnCl2 as additives., VAPOR DIFFUSION, HANGING DROP, temperature 293K |