4PBC
X-ray crystal structure of a putative D-amino acid aminotransferase from Burkholderia cenocepacia
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-06 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.080, 102.970, 152.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.771 - 1.800 |
| R-factor | 0.1693 |
| Rwork | 0.167 |
| R-free | 0.20690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.661 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9pre_1665)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.850 | |
| High resolution limit [Å] | 1.800 | 8.050 | 1.800 |
| Rmerge | 0.045 | 0.027 | 0.471 |
| Rmeas | 0.050 | 0.030 | 0.523 |
| Total number of observations | 333234 | ||
| Number of reflections | 63970 | 741 | 4655 |
| <I/σ(I)> | 20.09 | 44.24 | 3.39 |
| Completeness [%] | 98.0 | 87.5 | 97.8 |
| Redundancy | 5.21 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 400 nl protein solution + 400 nl precipitant solution. Precipitant was JCSG+ well H3 - 0.1 M BIS-TRIS pH 5.50, 25% PEG3350 |
