3BAS
Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9764 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 123.335, 44.912, 39.878 |
Unit cell angles | 90.00, 95.18, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.246 |
Rwork | 0.246 |
R-free | 0.28700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nkn |
RMSD bond length | 0.006 |
RMSD bond angle | 0.880 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 4.950 | 2.300 |
Rmerge | 0.082 | 0.044 | 0.245 |
Number of reflections | 8283 | ||
<I/σ(I)> | 9.9 | ||
Completeness [%] | 84.9 | 98.8 | 53.6 |
Redundancy | 3.3 | 3.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 277 | 1.5 microliter of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 3 microliters of (16.6% PEG 3350, 4.6% MPD, 13 mM NaCl, 2 mM NaN3, 10 mM MOPS pH 7.2) and equilibrated against (15% PEG 3350, 4.2% MPD, 18 mM MOPS, 24 mM NaCl), VAPOR DIFFUSION, HANGING DROP, temperature 277K |