3SJT
Crystal structure of human arginase I in complex with the inhibitor Me-ABH, Resolution 1.60 A, twinned structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-02-03 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 3 |
Unit cell lengths | 90.337, 90.337, 69.329 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.068 - 1.597 |
R-factor | 0.1301 |
Rwork | 0.129 |
R-free | 0.16310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zav |
RMSD bond length | 0.006 |
RMSD bond angle | 1.040 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.700 |
High resolution limit [Å] | 1.597 | 1.597 |
Rmerge | 0.050 | 0.298 |
Number of reflections | 82598 | |
<I/σ(I)> | 25.1 | 2.7 |
Completeness [%] | 95.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | 3 uL of protein solution [3.5 mg/mL HAI, 50 mM bicine (pH 8.5), 2 mM MABH, 100 M MnCl2] and 3 uL of precipitant solution [0.1 M HEPES (pH 7.0), 22-28% Jeffamine] were equilibrated against a 1 mL reservoir of precipitant solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K |