6M4E
Crystal structure of a GH1 beta-glucosidase from Hamamotoa singularis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-19 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 160.790, 172.830, 67.230 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.240 - 2.100 |
R-factor | 0.175 |
Rwork | 0.174 |
R-free | 0.19700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4gxp |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.290 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.110 | 1.775 |
Number of reflections | 55035 | 5423 |
<I/σ(I)> | 14.95 | 1.47 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 13.3 | 13 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1 M MIB Buffer pH 7.0, 25% (w/v) PEG 1500 |