4RHM
Crystal structure of T. brucei arginase-like protein quadruple mutant S149D/R151H/S153D/S226D
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 | 82.123, 137.350, 87.778 |
| Unit cell angles | 90.00, 102.28, 90.00 |
Refinement procedure
| Resolution | 42.880 - 1.950 |
| R-factor | 0.203 |
| Rwork | 0.201 |
| R-free | 0.23700 |
| Structure solution method | PHASER |
| Starting model (for MR) | 4rhk |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.778 |
| 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 | 2.010 |
| High resolution limit [Å] | 1.950 | 4.340 | 1.950 |
| Rmerge | 0.091 | ||
| Number of reflections | 64646 | ||
| <I/σ(I)> | 17.1 | ||
| Completeness [%] | 94.3 | 99.8 | 73.4 |
| Redundancy | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.2 M KNO3, 20% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
