8F8N
Crystal structure of the Arabidopsis SPIRAL2 C-terminal domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-02-09 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.9792603 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.480, 47.732, 111.113 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.799 - 1.798 |
| R-factor | 0.189 |
| Rwork | 0.186 |
| R-free | 0.21710 |
| Structure solution method | SAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.323 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.860 |
| High resolution limit [Å] | 1.798 | 3.880 | 1.800 |
| Rmerge | 0.098 | 0.050 | 0.194 |
| Number of reflections | 33280 | 3249 | 3158 |
| <I/σ(I)> | 12.7 | ||
| Completeness [%] | 98.0 | 95.1 | 92.1 |
| Redundancy | 5.6 | 5.6 | 3.2 |
| CC(1/2) | 0.994 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | Well solution (1ml) = 1.05 M Ammonium sulfate, 100 mM sodium acetate pH 4.6 Protein solution = 7 mg/ml protein in 25 mM Tris pH 8.5, 500 mM NaCl, and 0.1% beta-mercaptoethanol, 5 mM L-methionine Hanging drop = 2+2 microliters |






