9HE8
The molecular structure of a beta-1,4-D-xylosidase from the probiotic bacterium Levilactobacillus brevis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-10-24 |
| Detector | MAR CCD 300 mm |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.429, 177.180, 78.753 |
| Unit cell angles | 90.00, 98.84, 90.00 |
Refinement procedure
| Resolution | 47.045 - 1.898 |
| Rwork | 0.214 |
| R-free | 0.24130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.503 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.045 | 1.930 |
| High resolution limit [Å] | 1.898 | 1.900 |
| Rmerge | 0.153 | 0.898 |
| Rpim | 0.098 | 0.717 |
| Number of reflections | 163853 | 16853 |
| <I/σ(I)> | 10.6 | 1.2 |
| Completeness [%] | 98.1 | 87.5 |
| Redundancy | 3.4 | |
| CC(1/2) | 0.989 | 0.578 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293.15 | The best crystallisation conditions for the native protein were 27-29 % PEG 1500, 60 to 140 mM Malonate Imidazole Borate buffer, pH 4.0 to 4.5 |
