4RHK
Crystal structure of T. brucei arginase-like protein in an oxidized form
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 | 2012-10-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 153.148, 153.148, 85.426 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.657 - 2.380 |
| R-factor | 0.2282 |
| Rwork | 0.227 |
| R-free | 0.25600 |
| Structure solution method | PDB entry 4RHI |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.622 |
| 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 | 2.470 |
| High resolution limit [Å] | 2.380 | 5.130 | 2.380 |
| Rmerge | 0.101 | ||
| Number of reflections | 15468 | ||
| <I/σ(I)> | 31.429 | ||
| Completeness [%] | 99.9 | 99.6 | 99.8 |
| Redundancy | 18.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 294 | 2% (v/v) tacsimate, pH 7.4, 5% (v/v) 2-propanol, 0.1 M imidazole, 8% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 294K |






