5FR9
Structure of transaminase ATA-117 arRmut11 from Arthrobacter sp. KNK168 inhibited with 1-(4-Bromophenyl)-2-fluoroethylamine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04-1 |
| Synchrotron site | Diamond |
| Beamline | I04-1 |
| Temperature [K] | 120 |
| Detector technology | PIXEL |
| Collection date | 2015-11-28 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 84.148, 135.506, 197.319 |
| Unit cell angles | 90.00, 100.40, 90.00 |
Refinement procedure
| Resolution | 194.080 - 2.810 |
| R-factor | 0.21156 |
| Rwork | 0.210 |
| R-free | 0.23866 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wwj |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.464 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.520 | 2.860 |
| High resolution limit [Å] | 2.810 | 2.810 |
| Rmerge | 0.060 | 0.610 |
| Number of reflections | 105927 | |
| <I/σ(I)> | 15.5 | 2.1 |
| Completeness [%] | 99.4 | 99.7 |
| Redundancy | 4.2 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 22% (W/V) PEG 3350, 0.2 M MGCL2 IN 0.1 M BIS-TRIS PROPANE BUFFER PH 7.0. |
