4CE5
First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-09-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 105.670, 135.310, 116.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.483 - 1.630 |
| R-factor | 0.1386 |
| Rwork | 0.137 |
| R-free | 0.16690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ENSEMBLE OF SELECTED HOMOLOGOUS PROTEINS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.074 |
| Data reduction software | xia2 |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.640 | 1.690 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Rmerge | 0.090 | 0.720 |
| Number of reflections | 103737 | |
| <I/σ(I)> | 19.47 | 2.99 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.43 | 7.43 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
