5FO1
E301A 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 | 134.965, 134.965, 134.965 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.450 |
| R-factor | 0.21107 |
| Rwork | 0.209 |
| R-free | 0.25608 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x0k |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.160 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.720 | 2.580 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.080 | 0.480 |
| Number of reflections | 30328 | |
| <I/σ(I)> | 19 | 3 |
| Completeness [%] | 92.2 | 94.7 |
| Redundancy | 8.5 | 4.9 |
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 |
