5G2Q
The crystal structure of a S-selective transaminase from Arthrobacter sp. with alanine bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-17 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 1 |
| Unit cell lengths | 64.278, 99.814, 217.337 |
| Unit cell angles | 81.58, 89.12, 74.49 |
Refinement procedure
| Resolution | 47.960 - 2.300 |
| Rwork | 0.192 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gju |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.000 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.070 | 0.410 |
| Number of reflections | 214456 | |
| <I/σ(I)> | 8.5 | 1.8 |
| Completeness [%] | 93.8 | 87.5 |
| Redundancy | 2.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 15% PEG 3350 0.2 M NA-MALONATE 100 MM MMT BUFFER (DL-MALIC ACID, MES AND TRIS BASE) PH 5.0, 10 MM PLP |
