1LNZ
Structure of the Obg GTP-binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-04-24 |
Detector | CUSTOM-MADE |
Wavelength(s) | 0.9794 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.580, 105.006, 124.098 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 * - 2.600 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.29300 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.360 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | |
High resolution limit [Å] | 2.600 | |
Rmerge | 0.079 * | 0.320 * |
Total number of observations | 70639 * | |
Number of reflections | 38652 * | |
Completeness [%] | 82.5 * | 46.5 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 7-12% isopropanol, 0.1M magnesium chloride, 0.05M sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP at 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 13 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | reservoir | isopropanol | 7-12 (%) | |
6 | 1 | reservoir | 0.1 (M) | ||
7 | 1 | reservoir | sodium cacodylate | 0.05 (M) | pH6.5 |