8UFW
CA9 mimic with SLC compound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-06-13 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953659 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.985, 41.414, 72.309 |
| Unit cell angles | 90.00, 103.97, 90.00 |
Refinement procedure
| Resolution | 39.664 - 1.215 |
| Rwork | 0.113 |
| R-free | 0.14300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.763 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.400 | 1.240 |
| High resolution limit [Å] | 1.210 | 1.210 |
| Rmerge | 0.072 | 0.779 |
| Rpim | 0.030 | 0.326 |
| Number of reflections | 70793 | 3003 |
| <I/σ(I)> | 12.4 | 2.3 |
| Completeness [%] | 97.5 | 83.5 |
| Redundancy | 6.7 | 6.3 |
| CC(1/2) | 0.999 | 0.736 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | The protein was set up in MRC2 plates in 100 nL plus 100 nL drops with the protein at 5 mg/mL with reservoir solutions being 2.6 to 2.9 M ammonium sulfate and 100 mM Tris buffer at pH 8.3 to 8.9 |
