5AVO
Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NE3A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NE3A |
| Temperature [K] | 95 |
| Detector technology | PIXEL |
| Collection date | 2015-06-14 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.401, 79.472, 65.899 |
| Unit cell angles | 90.00, 107.16, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.2129 |
| Rwork | 0.211 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ydr |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.245 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | REFMAC |
| Refinement software | REFMAC (refmac_5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.062 | 0.048 | 0.261 |
| Rmeas | 0.078 | 0.060 | 0.328 |
| Rpim | 0.047 | 0.035 | 0.196 |
| Total number of observations | 119944 | ||
| Number of reflections | 47593 | ||
| <I/σ(I)> | 13.7 | ||
| Completeness [%] | 90.6 | 75.4 | 94.8 |
| Redundancy | 2.5 | 2.5 | 2.4 |
| CC(1/2) | 0.993 | 0.911 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | PEG 2000, magnesium chloride, PEG 400, 1,4-butanediol |
