3A22
Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2008-11-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.341, 99.283, 182.026 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.270 - 1.900 |
| R-factor | 0.16393 |
| Rwork | 0.162 |
| R-free | 0.20663 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3a21 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.212 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC (5.5.0088) |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.075 | 0.230 |
| Number of reflections | 97305 | |
| <I/σ(I)> | 31.7 | 12.2 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 9 | 8.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 1.7M ammonium sulfate, 1.7% PEG 400, 15% glycerol, 0.1M HEPES, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
