6NUN
Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER D8 QUEST |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-01-27 |
Detector | APEX II CCD |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 86.980, 86.980, 115.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.820 - 1.870 |
R-factor | 0.16282 |
Rwork | 0.161 |
R-free | 0.19844 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.494 |
Data reduction software | TRUNCATE |
Data scaling software | SAINT |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.820 | 1.910 |
High resolution limit [Å] | 1.870 | 1.870 |
Rmerge | 0.135 | 1.048 |
Rmeas | 0.141 | 1.110 |
Rpim | 0.042 | 0.358 |
Number of reflections | 42137 | 2604 |
<I/σ(I)> | 15.4 | 2.6 |
Completeness [%] | 99.5 | 92.1 |
Redundancy | 20.7 | 17.4 |
CC(1/2) | 0.999 | 0.838 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | 0.1 M LiCl, 0.1 MMES pH 6.0, 20% (m/v) PEG 6000 |