2DRM
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 |
Wavelength(s) | 0.86 |
Spacegroup name | P 1 |
Unit cell lengths | 29.969, 37.861, 44.506 |
Unit cell angles | 90.28, 90.11, 90.64 |
Refinement procedure
Resolution | 23.640 - 1.350 |
R-factor | 0.18678 |
Rwork | 0.186 |
R-free | 0.20626 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2drk |
RMSD bond length | 0.010 |
RMSD bond angle | 1.204 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.300 |
High resolution limit [Å] | 1.290 | 1.290 |
Rmerge | 0.020 | |
Number of reflections | 44074 | |
<I/σ(I)> | 16.6 | |
Completeness [%] | 89.4 | 53.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 280 | pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 280K |