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 |