3LP4
Crystal structure of human arginase I in complex with L-LYSINE, 1.90A Resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Detector technology | CCD |
Collection date | 2008-12-02 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 3 |
Unit cell lengths | 90.729, 90.729, 69.509 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.200 - 1.900 |
Rwork | 0.155 |
R-free | 0.20380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zav |
RMSD bond angle | 0.006 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.010 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.081 | 0.433 |
Number of reflections | 49010 | |
<I/σ(I)> | 17.4 | 2.5 |
Completeness [%] | 97.1 | 98.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 0.1 M bis-Tris pH 6.5, 28% PEGMME 2000. Crystals were harvested and soaked in a precipitant solution augmented with 20 mM L-lysine. Cryoprotected in 32% Jeffamine, VAPOR DIFFUSION, HANGING DROP |