6B05
The Crystal Structure of the Ferredoxin Protease FusC E83A mutant in complex with Arabidopsis Ferredoxin
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 | CCD |
| Collection date | 2017-03-08 |
| Detector | MAR CCD 130 mm |
| Wavelength(s) | 0.987 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 81.338, 126.505, 133.545 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.988 - 1.900 |
| R-factor | 0.1974 |
| Rwork | 0.195 |
| R-free | 0.23890 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.882 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | SHELXCD |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.790 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.100 | 1.637 |
| Rpim | 0.320 | 0.815 |
| Number of reflections | 108771 | 5302 |
| <I/σ(I)> | 20.1 | |
| Completeness [%] | 99.8 | 98.9 |
| Redundancy | 12.6 | 9.4 |
| CC(1/2) | 0.995 | 0.690 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20% PEG3350, 0.22M NaKPO4 |
