2BVD
HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES. STRUCTURE AND ACTIVITY OF A CLOSTRIDIUM THERMOCELLUM LICHENASE, CtLIC26A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-05 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.272, 63.012, 78.182 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.090 - 1.600 |
| R-factor | 0.156 |
| Rwork | 0.154 |
| R-free | 0.18600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bv9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.107 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.640 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.060 | 0.090 |
| Number of reflections | 32817 | |
| <I/σ(I)> | 26 | 17 |
| Completeness [%] | 99.0 | 98 |
| Redundancy | 6.5 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | PROTEIN WAS CO-CRYSTALLIZED WITH THE LIGAND FROM 0.15 M AMMONIUM SULPHATE, 30% PEG 5K MME BUFFERED TO PH 6.5 WITH MES |
