3MFV
Crystal structure of human arginase I in complex with 2-aminohomohistidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Detector technology | CCD |
| Collection date | 2008-12-01 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 3 |
| Unit cell lengths | 90.660, 90.660, 69.707 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.141 |
| Rwork | 0.141 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2zav |
| RMSD bond length | 0.008 |
| RMSD bond angle | 2.100 |
| 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 | 1.990 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.086 | 0.310 |
| Number of reflections | 50344 | |
| <I/σ(I)> | 15.4 | 3.8 |
| Completeness [%] | 99.8 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 3 uL of protein solution [3.5 mg/mL protein, 50 mM bicine (pH 8.5), 2 mM AHH, 100 M MnCl2] and 3 uL of precipitant solution [0.1 M HEPES (pH 7.0), 28% Jeffamine] were equilibrated against a 1 mL reservoir of precipitant solution. , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
