4CZ1
Crystal structure of kynurenine formamidase from Bacillus anthracis complexed with 2-aminoacetophenone.
Replaces: 4COAExperimental 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 | 2013-09-22 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.695, 66.561, 84.061 |
| Unit cell angles | 90.00, 90.24, 90.00 |
Refinement procedure
| Resolution | 42.640 - 2.240 |
| R-factor | 0.18576 |
| Rwork | 0.184 |
| R-free | 0.22410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4co9 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.684 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.640 | 2.320 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.160 | 0.550 |
| Number of reflections | 38046 | |
| <I/σ(I)> | 4.8 | 2.2 |
| Completeness [%] | 98.1 | 97.7 |
| Redundancy | 2.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 293 | 100 MM TRIS-HCL PH 8.5, 140 MM MGCL2 AND 30 % (W/V) PEG 4000. 293 K. PROTEIN WAS PREVIOUSLY INCUBATED WITH 5 % (V/V) 2-AMINOACETOPHENONE. |
