5Y5C
Crystal structure of dha bind to bovine beta-lactoglobulin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17B1 |
| Synchrotron site | SSRF |
| Beamline | BL17B1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-06-14 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97775 |
| Spacegroup name | P 32 |
| Unit cell lengths | 52.490, 52.490, 108.390 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.460 - 2.610 |
| R-factor | 0.20207 |
| Rwork | 0.200 |
| R-free | 0.24389 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gj5 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.651 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.500 |
| Rmerge | 0.085 |
| Number of reflections | 11464 |
| <I/σ(I)> | 24 |
| Completeness [%] | 98.4 |
| Redundancy | 9.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 289 | 1.34M trisodium citrate, 0.1M Tris |
