2AEB
Crystal structure of human arginase I at 1.29 A resolution and exploration of inhibition in immune response.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-04-20 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 3 |
Unit cell lengths | 91.422, 91.422, 69.637 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | ? - 1.290 |
R-free | 0.15200 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1d3v |
RMSD bond length | 0.012 |
RMSD bond angle | 0.030 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.340 |
High resolution limit [Å] | 1.290 | 1.290 |
Rmerge | 0.063 | 0.560 |
Number of reflections | 150499 | |
<I/σ(I)> | 9.6 | 1.85 |
Completeness [%] | 92.7 | 86 |
Redundancy | 1.4 | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.1 | 294 | PegMME 5000, Bis Tris, pH 7.1, VAPOR DIFFUSION, SITTING DROP, temperature 294.0K, pH 7.10 |