5FO0
D298E mutant of FAD synthetase from Corynebacterium ammoniagenes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-11 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 21 3 |
Unit cell lengths | 133.179, 133.179, 133.179 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.000 - 2.510 |
R-factor | 0.20567 |
Rwork | 0.203 |
R-free | 0.25078 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2x0k |
RMSD bond length | 0.007 |
RMSD bond angle | 1.216 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.090 | 2.650 |
High resolution limit [Å] | 2.510 | 2.510 |
Rmerge | 0.080 | 0.440 |
Number of reflections | 26982 | |
<I/σ(I)> | 24.7 | 4.6 |
Completeness [%] | 99.6 | 97.2 |
Redundancy | 10.6 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 1.5 M LI2SO4, 100 MM HEPES, PH 7.5 |