4C90
Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-18 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.390, 131.680, 199.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 62.600 - 2.650 |
R-factor | 0.20641 |
Rwork | 0.203 |
R-free | 0.26591 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.009 |
RMSD bond angle | 1.355 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXCDE |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.520 | 2.790 |
High resolution limit [Å] | 2.650 | 2.650 |
Rmerge | 0.130 | 0.500 |
Number of reflections | 219395 | |
<I/σ(I)> | 8.5 | 2.4 |
Completeness [%] | 97.5 | 94.5 |
Redundancy | 3.9 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 19% PEG3350, 0.2M SODIUM CITRATE PH 5.5 |