3FTN
Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii 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 | 79.376, 83.003, 119.691 |
Unit cell angles | 90.00, 99.93, 90.00 |
Refinement procedure
Resolution | 39.180 - 2.192 |
R-factor | 0.1663 |
Rwork | 0.165 |
R-free | 0.22820 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.090 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.240 |
High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
Rmerge | 0.092 | 0.058 | 0.349 |
Number of reflections | 76750 | ||
<I/σ(I)> | 11.597 | ||
Completeness [%] | 97.8 | 95.4 | 99.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 8 mg/mL protein, 25 mM Tris-HCl, 50 mM NaCl, 0.1 mM DTT, 50 mM ZnCl2 (pH=7.5)] was mixed with 1 microliter of reservoir solution [16% (w/v) PEG8K, 200 mM magnesium acetate tetrahydrate, 100 mM Cacodylate buffer (pH 6.5), vapor diffusion, hanging drop, temperature 298K |