2FXO
Structure of the human beta-myosin S2 fragment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-02-16 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 40.157, 41.867, 97.795 |
Unit cell angles | 91.11, 92.73, 107.18 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.277 |
Rwork | 0.273 |
R-free | 0.34900 |
Structure solution method | SAD WITH SEMI-BRUTE- FORCE MOLECULAR REPLACEMENT |
Starting model (for MR) | 1XNM |
RMSD bond length | 0.016 |
RMSD bond angle | 1.526 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 20190 | |
<I/σ(I)> | 9 | 3.2 |
Completeness [%] | 96.0 | 96.6 |
Redundancy | 3.2 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 296 | PEG 3350, SODIUM ACETATE, TRIS-HCL, pH 7.50, VAPOR DIFFUSION, SITTING DROP, temperature 296K |