1AS3
GDP BOUND G42V GIA1
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 1996-09 |
| Spacegroup name | I 4 |
| Unit cell lengths | 121.440, 121.440, 68.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.400 |
| R-factor | 0.212 |
| Rwork | 0.212 |
| R-free | 0.27400 |
| Structure solution method | DIFFERENCE FOURIER |
| Starting model (for MR) | 1gdd |
| RMSD bond length | 0.011 |
| RMSD bond angle | 23.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.063 | 0.330 |
| Number of reflections | 19384 | |
| <I/σ(I)> | 20.5 | |
| Completeness [%] | 99.3 | 99.2 |
| Redundancy | 3.6 |
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 5 MM GDP WAS THE BUFFER., vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5-7.5 (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) |
