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 |