3LP7
Crystal structure of Human Arginase I in complex with inhibitor N(omega)-hydroxy-L-arginine (NOHA), 2.04A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 3 |
Unit cell lengths | 90.680, 90.680, 69.820 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.220 - 2.040 |
R-factor | 0.123 |
Rwork | 0.123 |
R-free | 0.17400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zav |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.040 |
Rmerge | 0.089 |
Number of reflections | 40118 |
<I/σ(I)> | 28.9 |
Completeness [%] | 98.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | protein 3.5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM NOHA, 100 mM MnCl2] precipitant [0.1 M bis-Tris (pH 6.5), 28% PEGMME 2000], VAPOR DIFFUSION, HANGING DROP |