3UD6
Structural analyses of covalent enzyme-substrate analogue complexes reveal strengths and limitations of de novo enzyme design
Replaces: 3NL8Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-18 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 62.684, 62.684, 123.680 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.470 - 2.091 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a53 MODIFIED TO PREVENT MODEL BIAS |
RMSD bond length | 0.008 |
RMSD bond angle | 1.028 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.160 |
High resolution limit [Å] | 2.091 | 2.091 |
Number of reflections | 17137 | |
<I/σ(I)> | 22 | 6.86 |
Completeness [%] | 99.0 | 95.2 |
Redundancy | 2.9 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 5.5 | 298 | Protein at 5mg/ml in 100mm NaCl, 25mm TRIS pH7.5. Crystals grew at and near 2M ammonium sulfate, 4% PEG400, 100mN Na acetate pH5.5, vapor diffusion, temperature 298k, VAPOR DIFFUSION |