2EAD
Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with substrate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 100 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 88.448, 72.743, 129.207 |
| Unit cell angles | 90.00, 96.68, 90.00 |
Refinement procedure
| Resolution | 37.600 - 1.890 |
| R-factor | 0.16187 |
| Rwork | 0.159 |
| R-free | 0.20962 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.473 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 128.040 |
| High resolution limit [Å] | 1.890 |
| Number of reflections | 123029 |
| Completeness [%] | 97.5 |
| Redundancy | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 0.1M Tris (pH 7.5), 10% iso-propanol, 15% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
