1GIA
STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 80.600, 80.600, 106.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.175 |
| Rwork | 0.175 |
| R-free | 0.22800 |
| RMSD bond length | 0.010 * |
| RMSD bond angle | 1.381 * |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 * |
| High resolution limit [Å] | 2.000 * |
| Rmerge | 0.058 * |
| Total number of observations | 58811 * |
| Number of reflections | 24198 |
| Completeness [%] | 92.7 |
| Redundancy | 2.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6 * | 21 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25-30 (mg/ml) | |
| 2 | 1 | drop | 0.3 (mM) | ||
| 3 | 1 | drop | 5 (mM) | ||
| 4 | 1 | drop | 5 (mM) | ||
| 5 | 1 | drop | DTT | 10 (mM) | |
| 6 | 1 | drop | sodium acetate | 200 (mM) | |
| 7 | 1 | reservoir | ammonium sulfate | 1.8-1.9 (M) |






