7PXQ
GH115 alpha-1,2-glucuronidase D303A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-09-25 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9762 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 148.150, 148.150, 274.460 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.470 - 2.300 |
R-factor | 0.1918 |
Rwork | 0.190 |
R-free | 0.21890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4c90 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.901 |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHASER (1.19.2_4158) |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.470 | 2.382 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 79371 | 7781 |
<I/σ(I)> | 17.3 | |
Completeness [%] | 99.9 | |
Redundancy | 20 | |
CC(1/2) | 1.000 | 0.460 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.2 M CaCl2, 0.1 M HEPES pH 7.5 and 28% PEG400 |