2WBK
Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2008-09-17 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 91.447, 115.504, 97.705 |
| Unit cell angles | 90.00, 115.99, 90.00 |
Refinement procedure
| Resolution | 47.840 - 2.100 |
| R-factor | 0.172 |
| Rwork | 0.169 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2je8 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.710 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.5.0082) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 69.840 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.130 | 0.480 |
| Number of reflections | 106267 | |
| <I/σ(I)> | 11.7 | 4.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 14% PEG 3350, 0.1M MES PH 7.1, 0.2M NABR |
