4RHI
Crystal structure of SeMet-labeled wild-type T. brucei arginase-like protein in P321 space group
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 | 2013-07-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9788 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 139.009, 139.009, 90.509 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 42.360 - 2.550 |
R-factor | 0.2228 |
Rwork | 0.221 |
R-free | 0.26060 |
Structure solution method | SAD |
RMSD bond length | 0.003 |
RMSD bond angle | 0.628 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL2Map |
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 | 2.640 |
High resolution limit [Å] | 2.550 | 5.490 | 2.550 |
Number of reflections | 33070 | ||
Completeness [%] | 100.0 | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 294 | 0.1 M HEPES, pH 7.4, 10% PEG 3350, 5% 2-methyl-2,4-pentanediol, VAPOR DIFFUSION, SITTING DROP, temperature 294K |