6AOA
Monomeric crystal structure of the E497/C566D double mutant of the guanylyl cyclase domain of the RhoGC fusion protein from the aquatic fungus Blastocladiella emersonii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-10-27 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 34.350, 65.400, 88.440 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.883 - 1.400 |
| R-factor | 0.1908 |
| Rwork | 0.190 |
| R-free | 0.20790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ao9 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.810 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.111 | 0.423 |
| Number of reflections | 40049 | |
| <I/σ(I)> | 8.7 | 2.9 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 15% PEG20000, 10 mM potassium hydrogen tartrate |
