4BHT
Structural Determinants of Cofactor Specificity and Domain Flexibility in Bacterial Glutamate Dehydrogenases
Replaces: 2YFGExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.975, 152.861, 169.366 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.900 - 2.500 |
| R-factor | 0.1626 |
| Rwork | 0.159 |
| R-free | 0.22680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bvg |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.592 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.900 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.010 | 0.500 |
| Number of reflections | 91251 | |
| <I/σ(I)> | 18.1 | 3 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 5.9 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 15-25% PEG 3350, 0.1M HEPES/TRIS PH 7-8, 0.2M NACL |
