4EDQ
MBP-fusion protein of myosin-binding protein c residues 149-269
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-06-25 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97890 |
| Spacegroup name | P 1 |
| Unit cell lengths | 53.993, 60.700, 73.314 |
| Unit cell angles | 85.73, 79.20, 89.98 |
Refinement procedure
| Resolution | 39.277 - 1.641 |
| R-factor | 0.1731 |
| Rwork | 0.172 |
| R-free | 0.21450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q26 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.412 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.810 | 1.730 |
| High resolution limit [Å] | 1.640 | 1.640 |
| Rmerge | 0.069 | 0.418 |
| Number of reflections | 106790 | |
| <I/σ(I)> | 9.61 | 2.4 |
| Completeness [%] | 95.8 | 94.8 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9 | 290 | 20% PEG 5K MME 0.1 M Bicine pH 9.0 2.9mM 1-s-Nonyl- -D-thioglucoside, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
