1AS0
GTP-GAMMA-S BOUND G42V GIA1
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 1996-01 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 78.950, 78.950, 105.290 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.25900 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | 1gia |
RMSD bond length | 0.010 |
RMSD bond angle | 22.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 15.000 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.104 |
Number of reflections | 19678 |
<I/σ(I)> | 10.4 |
Completeness [%] | 75.0 |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 * | 20 * | THE PROTEIN WAS CRYSTALLIZED IN HANGING DROPS USING 4M (NH4)2SO3 AS THE PRECIPITANT. 50 MM HEPES, PH 8.0, 10 MM MGSO4, 10 MM DTT AND 0.2 MM GTP-GAMMA-S WAS THE BUFFER., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.5-10 (mg/ml) | |
2 | 1 | drop | 0.75-1.0 (M) | ||
3 | 1 | drop | sodium acetate | 50 (mM) | |
4 | 1 | reservoir | 1.5-2.0 (M) | ||
5 | 1 | reservoir | sodium acetate | 100 (mM) |