1GIL
STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS
Experimental procedure
Spacegroup name | P 32 2 1 |
Unit cell lengths | 80.500, 80.500, 106.550 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.300 |
R-factor | 0.23 * |
Rwork | 0.222 |
R-free | 0.31000 * |
RMSD bond length | 0.013 |
RMSD bond angle | 1.588 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 15.000 * |
High resolution limit [Å] | 2.300 * |
Rmerge | 0.041 * |
Total number of observations | 58697 * |
Number of reflections | 16167 |
Completeness [%] | 97.2 * |
Redundancy | 3.3 * |
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) |