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 |