4RHJ
Crystal structure of wild-type T. brucei arginase-like protein in a reduced 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 | 2014-07-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.075 |
Spacegroup name | P 3 |
Unit cell lengths | 139.243, 139.243, 90.167 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 42.229 - 1.800 |
R-factor | 0.2023 |
Rwork | 0.196 |
R-free | 0.23430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4rhi |
RMSD bond length | 0.009 |
RMSD bond angle | 1.182 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
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 | 1.860 |
High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
Number of reflections | 181427 | ||
Completeness [%] | 100.0 | 100 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 294 | 0.1 M HEPES, pH 7.8, 18% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 294K |