521P
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 40.500, 40.500, 161.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | ? - 2.600 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 4.030 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.600 * |
| Rmerge | 0.047 * |
| Total number of observations | 11868 * |
| Number of reflections | 5411 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 * | Scherer, A., (1989) J.Mol.Biol., 206, 257. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 3-4 (mg/ml) | |
| 2 | 1 | 1 | Tris-HCl | 64 (mM) | |
| 3 | 1 | 1 | dithioerithritol | 1 (mM) | |
| 4 | 1 | 1 | 10 (mM) | ||
| 5 | 1 | 1 | sodium azide | 1 (mM) | |
| 6 | 1 | 1 | PEG1450 | 20 (%(w/v)) |
