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 |
