3O48
Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 46.020, 46.020, 139.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.740 - 1.750 |
| R-factor | 0.16635 |
| Rwork | 0.165 |
| R-free | 0.18788 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pqn |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.853 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 5.000 | 1.800 |
| High resolution limit [Å] | 1.750 | 4.000 | 1.750 |
| Rmerge | 0.324 | 0.310 | 0.510 |
| Number of reflections | 15603 | ||
| <I/σ(I)> | 10.21 | 11.95 | 6.84 |
| Completeness [%] | 95.8 | ||
| Redundancy | 23.26 | 21.73 | 26.16 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 298 | 20% PEG 8000, 0.2M ammonium sulfate, 0.05 M Tris, 0.05 M NaCl, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
