3SC7
First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-23 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9797 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 95.090, 95.090, 130.560 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.570 - 1.500 |
R-factor | 0.19054 |
Rwork | 0.189 |
R-free | 0.21064 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.512 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.570 | 1.590 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.054 | |
Number of reflections | 108977 | |
Completeness [%] | 94.1 | 84.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1 M HEPES pH 7.5, 1.4 M K-Na tartrate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |