3SKK
Crystal structure of human arginase I in complex with the inhibitor FABH, Resolution 1.70 A, twinned structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 3 |
| Unit cell lengths | 90.094, 90.094, 69.362 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.779 - 1.701 |
| R-factor | 0.1401 |
| Rwork | 0.136 |
| R-free | 0.17790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zav |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.043 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.800 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.148 | 0.577 |
| Number of reflections | 66860 | |
| <I/σ(I)> | 11.6 | 2.3 |
| Completeness [%] | 99.0 | 98.2 |
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 FABH, 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 |
