4W4T
The crystal structure of the terminal R domain from the myxalamid PKS-NRPS biosynthetic pathway
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-01 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97920 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.838, 159.304, 54.897 |
| Unit cell angles | 90.00, 108.88, 90.00 |
Refinement procedure
| Resolution | 29.182 - 1.845 |
| R-factor | 0.1758 |
| Rwork | 0.175 |
| R-free | 0.21170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MAD data set collected of the same MxaA Reductase construct |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.028 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | |
| High resolution limit [Å] | 1.700 | 1.850 |
| Rmerge | 0.200 | |
| Number of reflections | 69238 | |
| <I/σ(I)> | 23 | 7.1 |
| Completeness [%] | 98.1 | 98.1 |
| Redundancy | 2.7 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 300 | 0.22M Ammonium Acetate, 28% PEG 3350, 0.1M Hepes pH 7.7 |
