4A6U
Crystal structure of the omega transaminase from Chromobacterium violaceum in the apo form, crystallised from PEG 3350
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-05-06 |
| Detector | MARRESEARCH SX-165 |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.170, 61.110, 60.240 |
| Unit cell angles | 109.14, 85.59, 103.25 |
Refinement procedure
| Resolution | 29.473 - 1.687 |
| R-factor | 0.1557 |
| Rwork | 0.154 |
| R-free | 0.17990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4a6r |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.116 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.070 | 0.420 |
| Number of reflections | 78926 | |
| <I/σ(I)> | 12.7 | 3.1 |
| Completeness [%] | 93.5 | 72.6 |
| Redundancy | 2.7 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.4 | 200 NL OF PROTEIN AT 12 MG/ML MIXED WITH 200NL OF 20 % W/V PEG 3350, 0.2 M NASCN, 0.1 M HEPES PH 7.5 |
