5GN1
Crystal structure of the C-terminal part of Fun30 ATPase domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-1A |
Synchrotron site | Photon Factory |
Beamline | BL-1A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-06-20 |
Detector | DECTRIS PILATUS 2M-F |
Wavelength(s) | 1.1000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 114.431, 118.394, 111.578 |
Unit cell angles | 90.00, 107.28, 90.00 |
Refinement procedure
Resolution | 36.205 - 1.950 |
R-factor | 0.1877 |
Rwork | 0.187 |
R-free | 0.21630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mwy |
RMSD bond length | 0.010 |
RMSD bond angle | 1.021 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 103556 | |
<I/σ(I)> | 20.73 | 2.13 |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.7 | 6.8 |
CC(1/2) | 0.860 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 289 | 0.1 M Sodium malonate, 12% PEG 3350 |