4XC7
Isobutyryl-CoA mutase fused with bound butyryl-CoA and without cobalamin or GDP (apo-IcmF)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-08-02 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.9792 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 318.180, 318.180, 344.710 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 91.851 - 3.450 |
| R-factor | 0.1873 |
| Rwork | 0.186 |
| R-free | 0.20340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xc6 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.557 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_1760)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 3.540 |
| High resolution limit [Å] | 3.450 | 3.450 |
| Number of reflections | 84003 | |
| <I/σ(I)> | 11.7 | 3.8 |
| Completeness [%] | 95.7 | 55.4 |
| Redundancy | 10.4 | 10.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | precipitant: 700 - 750 mM sodium potassium tartrate, 100 mM tris pH 8.5 protein in 50 mM NaCl, 20 mM HEPES pH 8, 10 mM butyryl-CoA, mixed with precipitant 1 uL + 1 uL |
