4RHQ
Crystal structure of T. brucei arginase-like protein double mutant S149D/S153D
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 83.184, 138.060, 90.937 |
| Unit cell angles | 90.00, 101.98, 90.00 |
Refinement procedure
| Resolution | 44.479 - 2.180 |
| R-factor | 0.2065 |
| Rwork | 0.205 |
| R-free | 0.23790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4rhk |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.697 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.3_1479)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.260 |
| High resolution limit [Å] | 2.180 | 4.700 | 2.180 |
| Rmerge | 0.127 | ||
| Number of reflections | 51646 | ||
| <I/σ(I)> | 13.2 | ||
| Completeness [%] | 99.9 | 100 | 99.3 |
| Redundancy | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.2 M KF, 20% (v/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
