5B5H
Hydrophobic ice-binding site confer hyperactivity on antifreeze protein from a snow mold fungus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-17A |
| Synchrotron site | Photon Factory |
| Beamline | BL-17A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-12-12 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.98000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 48.388, 104.849, 35.626 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 52.400 - 1.000 |
| R-factor | 0.12098 |
| Rwork | 0.120 |
| R-free | 0.13578 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vn3 |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.269 |
| Data reduction software | HKL-2000 (2.3.9) |
| Data scaling software | HKL-2000 (2.3.9) |
| Phasing software | PHENIX (1.9-1692) |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.400 | 1.060 |
| High resolution limit [Å] | 1.000 | 1.000 |
| Rmerge | 0.091 | 0.419 |
| Number of reflections | 83006 | |
| <I/σ(I)> | 4.8 | 1.5 |
| Completeness [%] | 84.5 | 24.6 |
| Redundancy | 10.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1 M MES monohydrate, 1.6 M ammonium sulfate, 10%(v/v) 1,4-dioxane |
