8TFO
Structure of MKvar
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-06 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.953723 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.081, 80.705, 207.467 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.091 - 2.000 |
| Rwork | 0.208 |
| R-free | 0.24710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.262 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0415) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.100 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.292 | 4.656 |
| Rpim | 0.057 | 0.900 |
| Number of reflections | 52511 | 3787 |
| <I/σ(I)> | 11.8 | 1 |
| Completeness [%] | 99.8 | 97.5 |
| Redundancy | 27.1 | 26.8 |
| CC(1/2) | 0.999 | 0.623 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.4 | 293 | Protein bound to mevalonate at about 3 mg/mL was set up in 150 nL plus 150 nL drops over 50 microlitres of reservoir which contained: 0.126 M calcium acetate, 24.9 v/v PEG 400, 0.09 M sodium HEPES pH 8.4 with 10 mM taurine |
