1GIT
STRUCTURE OF GTP-BINDING PROTEIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F2 |
Synchrotron site | CHESS |
Beamline | F2 |
Detector technology | IMAGE PLATE |
Collection date | 1993 |
Detector | FUJI |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 77.100, 77.100, 144.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.600 |
R-factor | 0.186 |
Rwork | 0.186 |
R-free | 0.27900 |
RMSD bond length | 0.011 |
RMSD bond angle | 22.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 * | |
High resolution limit [Å] | 2.600 * | |
Rmerge | 0.030 * | 0.090 * |
Total number of observations | 28864 * | |
Number of reflections | 11856 | |
Completeness [%] | 84.1 | 86.5 * |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 * | 20 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-10 (mg/ml) | |
2 | 1 | drop | 2.5 (mM) | ||
3 | 1 | drop | EDTA | 0.25 (mM) | |
4 | 1 | drop | dithiothreitol | 2.5 (mM) | |
5 | 1 | drop | GTPgammaS | 2.5 (mM) | |
6 | 1 | drop | NaEPPS | 12.5 (mM) | |
7 | 1 | drop | ammonium sulfate | 1.1-1.25 (M) | |
8 | 1 | reservoir | ammonium sulfate | 2.2-2.5 (M) |