3WNQ
Crystal structure of (R)-carbonyl reductase H49A mutant from Candida Parapsilosis in complex with 2-hydroxyacetophenone
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-01-13 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.329, 93.028, 242.353 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.950 |
| R-factor | 0.233 |
| Rwork | 0.230 |
| R-free | 0.28800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wlf |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.510 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.060 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.087 | 0.498 |
| Number of reflections | 34016 | |
| <I/σ(I)> | 20.2 | 3 |
| Completeness [%] | 99.2 | 99.2 |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | 0.1M BIS-TRIS, 18%(w/v) PEG1500, 8%(w/v) PEG3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
