4XSH
The complex structure of C3cer exoenzyme and GTP bound RhoA (NADH-bound state)
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 | 2014-09-30 |
| Detector | RIGAKU RAXIS VII |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 32 |
| Unit cell lengths | 50.424, 50.424, 136.667 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.560 - 2.500 |
| R-factor | 0.19589 |
| Rwork | 0.190 |
| R-free | 0.25353 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1A2B and 3BW8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.259 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX (1.9) |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 13464 |
| <I/σ(I)> | 21 |
| Completeness [%] | 99.9 |
| Redundancy | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 100 mM MES (pH 6.4), 20% PEG1500 |
