2Q21
CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP
Replaces: 3P21Experimental procedure
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 83.200, 83.200, 105.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.200 |
| R-factor | 0.192 * |
| Rwork | 0.192 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.500 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.200 * |
| Rmerge | 0.081 * |
| Total number of observations | 48073 * |
| Number of reflections | 10447 * |
| Completeness [%] | 80.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 * | took Jancarik et al., 1988 from original paper * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | Hepes | 75 (mM) | |
| 2 | 1 | 1 | 100 (mM) | ||
| 3 | 1 | 1 | EDTA | 0.5 (mM) | |
| 4 | 1 | 1 | dithiothreitol | 0.5 (mM) | |
| 5 | 1 | 1 | n-octylglucoside | 0.005 (%) | |
| 6 | 1 | 2 | PEG400 | 30 (%) |
