1WVB
Crystal structure of human arginase I: the mutant E256Q
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-05-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 3 |
Unit cell lengths | 90.272, 90.272, 69.305 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.300 |
R-factor | 0.154 |
Rwork | 0.154 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1d3v |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.108 | |
Number of reflections | 27626 | |
<I/σ(I)> | 12.1 | 2.7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 3.6 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | PEGMME 2000, Bis-tris, ph 6.5(reservoir), pH 8.5(SAMPLE), VAPOR DIFFUSION, HANGING DROP, temperature 298K |