5FGU
Structure of Sda1 nuclease apoprotein as an EGFP fixed-arm fusion
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 93.15 |
| Detector technology | CCD |
| Collection date | 2015-02-19 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 81.407, 139.373, 120.970 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.276 - 1.896 |
| R-factor | 0.178 |
| Rwork | 0.177 |
| R-free | 0.20120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | EGFP component of 4JRB |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.217 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.896 | 1.896 |
| Rmerge | 0.610 | |
| Number of reflections | 54586 | |
| <I/σ(I)> | 25.6 | 3.54 |
| Completeness [%] | 100.0 | 99.6 |
| Redundancy | 7.3 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | Crystals were grown by mixing 0.25uL of protein (13.3mg/mL) with 0.25uL mother liquor (45mM Na cacodylate pH 6, 13.5mM magnesium sulfate, 1.53M ammonium sulfate), using sitting drop vapor diffusion |
