4AQ6
substrate bound homogentisate 1,2-dioxygenase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 1 |
Unit cell lengths | 93.393, 93.714, 162.984 |
Unit cell angles | 87.69, 80.42, 68.39 |
Refinement procedure
Resolution | 34.174 - 1.980 |
R-factor | 0.1639 |
Rwork | 0.161 |
R-free | 0.21620 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eyb |
RMSD bond length | 0.007 |
RMSD bond angle | 1.062 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 2.030 |
High resolution limit [Å] | 1.980 | 1.980 |
Rmerge | 0.100 | 0.590 |
Number of reflections | 337386 | |
<I/σ(I)> | 9.2 | 1.9 |
Completeness [%] | 95.6 | 91.5 |
Redundancy | 2.9 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8 | VAPOUR DIFFUSION (1:1 MIX): 17 % PEG 3350, 0.02 M NAK PHOSPHATE AND 0.1 M BIS-TRIS PROPANE PH 8.0, 1 MM TCEP, 2 MICROMETER HOMOGENTISATE, 15 MG/ML PROTEIN |