4C91
Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-10-16 |
Detector | DECTRIS PILATUS 6M-F |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.040, 130.290, 190.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.740 - 2.140 |
R-factor | 0.17618 |
Rwork | 0.174 |
R-free | 0.21878 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | APO FORM SEE PAPER |
RMSD bond length | 0.016 |
RMSD bond angle | 1.622 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.430 | 2.260 |
High resolution limit [Å] | 2.140 | 2.140 |
Rmerge | 0.100 | 0.420 |
Number of reflections | 93249 | |
<I/σ(I)> | 9.3 | 2.5 |
Completeness [%] | 94.4 | 91.5 |
Redundancy | 2.9 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 19% PEG3350, 0.2M SODIUM CITRATE PH 5.5 |