3WWH
Crystal structure of the first R-stereoselective -transaminase identified from Arthrobacter sp. KNK168 (FERM-BP-5228)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-30 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 80.620, 80.620, 93.880 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.310 - 1.650 |
| R-factor | 0.15426 |
| Rwork | 0.153 |
| R-free | 0.17243 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.209 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.750 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Number of reflections | 37725 | |
| Completeness [%] | 99.8 | 98.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 293 | 0.2 M magnesium chloride, 0.1 M Bis-Tris, 22% (w/v) PEG 3350, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
