3FPC
Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-06-17 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.742, 82.429, 118.249 |
| Unit cell angles | 90.00, 99.89, 90.00 |
Refinement procedure
| Resolution | 48.770 - 1.400 |
| R-factor | 0.118 |
| Rwork | 0.116 |
| R-free | 0.15500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kev |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.507 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.075 | 0.664 |
| Number of reflections | 294442 | |
| <I/σ(I)> | 20.143 | 1.4 |
| Completeness [%] | 99.3 | 93 |
| Redundancy | 3.1 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 8mg/mL protein [25mM Tris-HCl, 50mM NaCl, 0.1mM DTT, 50mM ZnCl2 (pH=7.5)] was mixed with 0.001 ml of reservoir solution [16% (w/v) PEG 8000, 200mM magnesium acetate tetrahydrate, 100mM Cacodylate buffer (pH 6.5)], vapor diffusion, hanging drop, temperature 298K |
