6CMZ
2.3 Angstrom Resolution Crystal Structure of Dihydrolipoamide Dehydrogenase from Burkholderia cenocepacia in Complex with FAD and NAD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-02-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 83.565, 107.246, 105.427 |
| Unit cell angles | 90.00, 106.09, 90.00 |
Refinement procedure
| Resolution | 29.210 - 2.300 |
| R-factor | 0.20144 |
| Rwork | 0.199 |
| R-free | 0.25320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lvl |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.466 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MoRDa |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.109 | 0.791 |
| Rmeas | 0.124 | 0.909 |
| Rpim | 0.059 | 0.443 |
| Number of reflections | 79190 | 3954 |
| <I/σ(I)> | 13.2 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.4 | 4.1 |
| CC(1/2) | 0.624 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 295 | Protein: 8.0 mg/ml, 0.5 Sodium chloride, 0.01M Tris pH 8.3, 1mM FAD; Screen: PACT (D1), 0.1M MMT buffer pH 4.0, 25% (w/v) PEG 1500 |
