6A9C
Crystal Structure c-terminal SH3 domain of Myosin IB from Entamoeba histolytica bound to EhFP10(GEF) peptide.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2015-04-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 29.008, 60.013, 95.305 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.780 - 1.980 |
| R-factor | 0.20307 |
| Rwork | 0.201 |
| R-free | 0.24009 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5xgg |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.870 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.780 | 2.010 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.103 | |
| Number of reflections | 12177 | 1153 |
| <I/σ(I)> | 27.76 | 3.3 |
| Completeness [%] | 100.0 | |
| Redundancy | 14 | |
| CC(1/2) | 0.900 | 0.980 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.2M Ammonium sulphate, 30% PEG 8000 |






