1HQX
R308K ARGINASE VARIANT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.946445 |
Spacegroup name | P 32 |
Unit cell lengths | 87.860, 87.860, 112.100 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.263 * |
Rwork | 0.263 |
R-free | 0.29600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.100 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.089 | 0.309 |
Total number of observations | 69842 * | |
Number of reflections | 18649 | |
<I/σ(I)> | 7.5 | |
Completeness [%] | 96.0 | 81.3 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 4 * | Kanyo, Z.F., (1992) J.Mol.Biol., 224, 1175. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | Bicine | 50 (mM) | |
3 | 1 | drop | 1 (mM) | ||
4 | 1 | reservoir | PEG8000 | 14 (%(w/v)) | |
5 | 1 | reservoir | Bicine | 50 (mM) | |
6 | 1 | reservoir | 1 (mM) | ||
7 | 1 | reservoir | sodium azide | 0.05 (%(w/v)) |