5XG9
Crystal Structure of PEG-bound SH3 domain of Myosin IB from Entamoeba histolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-27 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.462, 79.611, 88.479 |
| Unit cell angles | 90.00, 122.65, 90.00 |
Refinement procedure
| Resolution | 74.500 - 1.780 |
| R-factor | 0.18485 |
| Rwork | 0.183 |
| R-free | 0.22804 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5xgg |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.930 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.500 | 1.810 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Rmerge | 0.471 | |
| Rmeas | 0.550 | |
| Rpim | 0.280 | |
| Number of reflections | 58363 | |
| <I/σ(I)> | 17.2 | 2.3 |
| Completeness [%] | 98.9 | 100 |
| Redundancy | 3.8 | 3.8 |
| CC(1/2) | 0.840 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 0.2M Ammonium sulphate, 30% PEG 8000 |
