9N4B
RhoA GTPase R70A bound to GTPgammaS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2016-08-16 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 59.988, 59.988, 150.756 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.410 - 3.000 |
| R-factor | 0.2042 |
| Rwork | 0.199 |
| R-free | 0.24670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.161 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.19.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.410 | 3.107 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.054 | 0.236 |
| Rmeas | 0.077 | |
| Number of reflections | 13211 | 1150 |
| <I/σ(I)> | 10.82 | 2.41 |
| Completeness [%] | 94.4 | 86.61 |
| Redundancy | 1.8 | 1.7 |
| CC(1/2) | 0.998 | 0.950 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 2 uL protein (8 mg/mL RhoA R70A bound to GTPgammaS in 25 mM Tris-HCl pH8.0, 2 mM MgCl2, and 10 mM BME) + 2 uL crystallization reagent sitting above 500 uL crystallization reagent. Crystallization reagent: 250 mM ammonium sulfate, 1.50 M lithium sulfate, and 100 mM sodium citrate pH 5.6 |






