5G2P
The crystal structure of a S-selective transaminase from Arthrobacter sp.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-06 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.398, 142.662, 99.681 |
| Unit cell angles | 90.00, 105.33, 90.00 |
Refinement procedure
| Resolution | 46.840 - 1.890 |
| R-factor | 0.15882 |
| Rwork | 0.157 |
| R-free | 0.20048 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gju |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.403 |
| 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] | 48.100 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.090 | 0.640 |
| Number of reflections | 137172 | |
| <I/σ(I)> | 14.1 | 2.2 |
| Completeness [%] | 99.8 | 92.4 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 15% PEG3350 0.2 M NA-MALONATE 100 MM MMT BUFFER (DL-MALIC ACID, MES AND TRIS BASE) PH 5.0) 10 MM PLP |
