6F4L
Structure of quinolinate synthase with inhibitor-derived quinolinate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-09 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.96770 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.440, 49.310, 61.900 |
| Unit cell angles | 90.00, 107.21, 90.00 |
Refinement procedure
| Resolution | 46.950 - 2.300 |
| R-factor | 0.2029 |
| Rwork | 0.202 |
| R-free | 0.22040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4p3x |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.373 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.27) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.950 | 46.950 | 2.380 |
| High resolution limit [Å] | 2.300 | 8.910 | 2.300 |
| Rmerge | 0.137 | 0.049 | 1.775 |
| Rmeas | 0.152 | 0.055 | 1.962 |
| Rpim | 0.064 | 0.024 | 0.825 |
| Total number of observations | 77646 | 1316 | 8006 |
| Number of reflections | 14259 | 267 | 1412 |
| <I/σ(I)> | 8.9 | 45.5 | 1 |
| Completeness [%] | 99.1 | 98.3 | 99.7 |
| Redundancy | 5.4 | 4.9 | 5.7 |
| CC(1/2) | 0.996 | 0.997 | 0.375 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 9.1 | 298 | PEG33500, Na2HPO4, CHES, anaerobic |
