2YFQ
Crystal structure of Glutamate dehydrogenase from Peptoniphilus asaccharolyticus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-15 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 153.314, 153.314, 318.993 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.940 |
| R-factor | 0.24389 |
| Rwork | 0.242 |
| R-free | 0.28693 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.439 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | Auto-Rickshaw |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.010 |
| High resolution limit [Å] | 2.940 | 2.940 |
| Rmerge | 0.120 | 0.590 |
| Number of reflections | 58934 | |
| <I/σ(I)> | 18.7 | 2.9 |
| Completeness [%] | 99.8 | 97.8 |
| Redundancy | 11.5 | 8.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 0.1 M SODIUM CACODYLATE PH 6.5, 200 MM NACL |
