2DRK
Acanthamoeba myosin I SH3 domain bound to Acan125
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-06-30 |
| Wavelength(s) | 0.86 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.701, 37.362, 43.836 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.400 - 1.420 |
| R-factor | 0.159 |
| Rwork | 0.159 |
| R-free | 0.17300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sem |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.142 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.460 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Number of reflections | 10624 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 278 | pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 278K |
