5YEQ
The structure of Sac-KARI protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-03-26 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.434, 90.827, 154.105 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.062 - 1.750 |
| R-factor | 0.17662 |
| Rwork | 0.175 |
| R-free | 0.21585 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xdz |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.050 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 78.250 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Number of reflections | 69217 | 6734 |
| <I/σ(I)> | 33.8 | |
| Completeness [%] | 99.4 | 98.7 |
| Redundancy | 4.4 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 298 | 0.2 M Li2SO4 and 20% PEG3350 |
