6EIO
Crystal structure of an ice binding protein from an Antarctic Biological Consortium
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-20 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.82656 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.482, 50.717, 92.452 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.226 - 0.840 |
| R-factor | 0.1155 |
| Rwork | 0.115 |
| R-free | 0.12800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wp9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.167 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.230 | 0.890 |
| High resolution limit [Å] | 0.840 | 0.840 |
| Rmerge | 0.110 | 0.580 |
| Number of reflections | 183816 | 19237 |
| <I/σ(I)> | 10 | 1.8 |
| Completeness [%] | 94.5 | 68.8 |
| Redundancy | 5.5 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 2.2 M (NH4)2SO4, 0.1 M HEPES pH 7.5 |
