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 |
