7WUD
An (R)-Selective Transaminase mutant
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 | 2020-10-31 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.762, 141.476, 88.388 |
| Unit cell angles | 90.00, 99.88, 90.00 |
Refinement procedure
| Resolution | 37.270 - 1.900 |
| R-factor | 0.191 |
| Rwork | 0.189 |
| R-free | 0.23080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7dbe |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.781 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.099 | |
| Number of reflections | 117747 | 5899 |
| <I/σ(I)> | 23.1 | |
| Completeness [%] | 100.0 | |
| Redundancy | 6.9 | |
| CC(1/2) | 0.967 | 0.891 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 2% v/v Tacsimate, pH 7.0, 0.1M Tris-HCl, pH 8.0, 24% w/v Polyethylene glycol 3350 |
