8UFX
CAII 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 | 42.471, 41.375, 71.827 |
| Unit cell angles | 90.00, 104.38, 90.00 |
Refinement procedure
| Resolution | 40.068 - 1.212 |
| Rwork | 0.124 |
| R-free | 0.14740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.761 |
| 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 | 1.230 |
| High resolution limit [Å] | 1.210 | 1.210 |
| Rmerge | 0.102 | 0.904 |
| Rpim | 0.043 | 0.397 |
| Number of reflections | 71738 | 2235 |
| <I/σ(I)> | 8.7 | 1.7 |
| Completeness [%] | 97.8 | 62.8 |
| Redundancy | 6.5 | 5.5 |
| CC(1/2) | 0.996 | 0.632 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 281 | The protein was set up in MRC-2 plates (Molecular Dimensions, Sheffield, UK) using a Phoenix robot (Art Robbins Instruments, Sunnyvale, CA, USA) in 250 nL plus 250 nL drops with the protein at 4.2 mg/mL with the reservoir solutions being 2.5 to 2.8 M ammonium sulfate and 50 to 100 mM Tris buffer pH 8.1 to 8.9 |
