1HQG
CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-06-19 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.08 |
Spacegroup name | P 32 |
Unit cell lengths | 88.200, 88.200, 106.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.243 |
Rwork | 0.243 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 22.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.061 | 0.350 |
Total number of observations | 111757 * | |
Number of reflections | 59154 | |
<I/σ(I)> | 12.2 | |
Completeness [%] | 94.3 | 96.9 |
Redundancy | 1.9 | 1.9 |
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)) |