5LVW
XiaF (FADH2) from Streptomyces sp.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-12-10 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 166.600, 166.600, 99.660 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.900 |
R-factor | 0.17504 |
Rwork | 0.174 |
R-free | 0.20199 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2jbr |
RMSD bond length | 0.004 |
RMSD bond angle | 0.846 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.084 | 0.525 |
Number of reflections | 17733 | |
<I/σ(I)> | 18.8 | 5.9 |
Completeness [%] | 95.3 | 96.9 |
Redundancy | 9.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1,6 M ammonium sulfate, 0.1 M HEPES, 0.1 M sodium chloride, 0.5 M NADH, 0.15 M FAD. anaerobic crystallization. 0.5 uM XiaP (protein, reductase) |