4COG
Crystal structure of kynurenine formamidase from Burkholderia cenocepacia
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-09-23 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 76.859, 50.120, 135.197 |
| Unit cell angles | 90.00, 94.15, 90.00 |
Refinement procedure
| Resolution | 134.840 - 1.600 |
| R-factor | 0.15063 |
| Rwork | 0.149 |
| R-free | 0.18431 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | KYNURENINE FORMAMIDASE FROM PSEUDOMONAS AERUGINOSA |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.422 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.370 | 1.690 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.070 | 0.480 |
| Number of reflections | 134904 | |
| <I/σ(I)> | 12.8 | 3 |
| Completeness [%] | 99.3 | 99.8 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 293 | 14 % (W/V) PEG 3350, 5 MM COCL2, 5 MM CDCL2, 5 MM MGCL2 AND 5 MM NICL2. 293 K. |
