2FRD
Structure of Transhydrogenase (dI.S138A.NADH)2(dIII.NADPH)1 asymmetric complex
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 | 2004-02-22 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.300, 74.110, 205.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.930 - 3.200 |
| R-factor | 0.21852 |
| Rwork | 0.213 |
| R-free | 0.27230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hzz |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.217 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.930 | 3.370 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.072 | 0.326 |
| Number of reflections | 18400 | |
| <I/σ(I)> | 13.4 | 4 |
| Completeness [%] | 98.9 | 99.2 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | 22-24% 8K-PEG, 60-140 mM (NH4)2SO4, 100 mM Mes, pH 6.0 and 10% glycerol in the presence of 50 mM NADH and 5 mM NADPH, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
