3FSR
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 | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-08-11 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 79.291, 101.427, 113.169 |
Unit cell angles | 90.00, 94.19, 90.00 |
Refinement procedure
Resolution | 39.418 - 2.200 |
R-factor | 0.164 |
Rwork | 0.161 |
R-free | 0.22000 |
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 | 0.109 | 0.032 | 0.620 |
Number of reflections | 90320 | ||
<I/σ(I)> | 11.363 | ||
Completeness [%] | 99.7 | 97.1 | 100 |
Redundancy | 2.5 |
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 0.001ml of reservoir solution [16% (w/v) PEG 8000, 200mM magnesium acetate tetrahydrate, 100mM Cacodylate buffer (pH 6.5)], vapor diffusion, hanging drop, temperature 298K |