5ZFM
Ketoreductase LbCR mutant - M6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-06-09 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.97775 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.338, 116.052, 75.183 |
Unit cell angles | 90.00, 114.33, 90.00 |
Refinement procedure
Resolution | 44.278 - 2.000 |
R-factor | 0.1602 |
Rwork | 0.158 |
R-free | 0.19460 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.995 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.280 | 2.071 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.197 | 0.516 |
Number of reflections | 72544 | |
<I/σ(I)> | 10.143 | |
Completeness [%] | 99.1 | |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | PEG 4000, MES buffer, sodium chloride, glycyl-glycyl-glycine |