6FPG
Structure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellin
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 | PIXEL |
| Collection date | 2017-09-22 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 1 |
| Unit cell lengths | 59.507, 85.660, 95.785 |
| Unit cell angles | 96.16, 92.39, 90.37 |
Refinement procedure
| Resolution | 48.497 - 1.800 |
| R-factor | 0.188 |
| Rwork | 0.186 |
| R-free | 0.21640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6fpf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.201 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.041 | 0.472 |
| Number of reflections | 168279 | 16605 |
| <I/σ(I)> | 11.2 | 1.6 |
| Completeness [%] | 96.6 | 95.1 |
| Redundancy | 2.9 | 2.9 |
| CC(1/2) | 0.990 | 0.700 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 294 | 0.1 M sodium citrate pH 5.5, 15 % (w/v) PEG 6000 |
