1WER
RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID2 |
| Synchrotron site | ESRF |
| Beamline | ID2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-03-26 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.200, 55.600, 142.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 5.000 - 1.600 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.27100 |
| Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 22.400 * |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.064 | 0.200 |
| Number of reflections | 42457 | |
| <I/σ(I)> | 15.4 | 6.7 |
| Completeness [%] | 98.0 | 97 |
| Redundancy | 3.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | micro-seeding * | 6.5 | SEE REFERENCE 1, pH 6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | PEG3350 | 7-8.5 (%) | |
| 3 | 1 | drop | MES | 50 (mM) | |
| 4 | 1 | drop | 100 (mM) | ||
| 5 | 1 | reservoir | MES | 100 (mM) | |
| 6 | 1 | reservoir | PEG3350 | 14-17 (%) | |
| 7 | 1 | reservoir | 200 (mM) |
