5VT9
Myosin Light chain 1 and MyoA complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-02-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.127 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.990, 64.390, 65.150 |
Unit cell angles | 90.00, 97.72, 90.00 |
Refinement procedure
Resolution | 40.618 - 1.850 |
R-factor | 0.1928 |
Rwork | 0.191 |
R-free | 0.22940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qac |
RMSD bond length | 0.005 |
RMSD bond angle | 0.949 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.560 | 1.890 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.076 | 0.627 |
Number of reflections | 28665 | 1749 |
<I/σ(I)> | 15.3 | 2.9 |
Completeness [%] | 99.6 | 99.8 |
Redundancy | 6 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 0.9 uL 8 mg/mL protein + 1.35 uL reservoir (0.1 M Bis-Tris, pH 5.5, 25% PEG3350) |