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 |