4CFQ
Ca-bound truncated (delta13C) and C3S, C81S and C86S mutated S100A4 complexed with non-muscle myosin IIA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-09-11 |
| Spacegroup name | P 1 |
| Unit cell lengths | 38.720, 38.790, 71.430 |
| Unit cell angles | 88.65, 75.54, 72.17 |
Refinement procedure
| Resolution | 31.772 - 1.370 |
| R-factor | 0.162 |
| Rwork | 0.161 |
| R-free | 0.19280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zwh |
| RMSD bond length | 0.035 |
| RMSD bond angle | 1.873 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 31.800 | 1.440 |
| High resolution limit [Å] | 1.370 | 1.370 |
| Rmerge | 0.070 | 0.550 |
| Number of reflections | 79285 | |
| <I/σ(I)> | 10.9 | 2.2 |
| Completeness [%] | 98.5 | 94.5 |
| Redundancy | 3.5 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 0.1 M MIB, PH 4, 25% W/V PEG 1500 |
