1NZN
Cytosolic domain of the human mitchondrial fission protein Fis1 adopts a TPR fold
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2002-12-13 |
| Detector | SBC-2 |
| Wavelength(s) | 0.96446 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 48.985, 48.985, 169.199 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| Rwork | 0.230 |
| R-free | 0.25500 * |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.085 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 * | 2.050 |
| High resolution limit [Å] | 2.500 * | 2.000 |
| Rmerge | 0.044 * | |
| Number of reflections | 7912 * | |
| Completeness [%] | 99.7 * | 99.8 |
| Redundancy | 7. * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 298 | Ammonium Sulphate, Sodium Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 32 (mg/ml) | |
| 2 | 1 | drop | sodium acetate | 25 (mM) | |
| 3 | 1 | drop | dithiothreitol | 2 (mM) | pH5.0 |
| 4 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
| 6 | 1 | reservoir | glycerol | 5 (%) | pH4.6 |
