3O6Y
Robust computational design, optimization, and structural characterization of retroaldol enzymes
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2009-07-01 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 62.598, 62.598, 123.698 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 54.230 - 2.091 |
| R-factor | 0.23582 |
| Rwork | 0.233 |
| R-free | 0.29088 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1A53 with designed and adjacent residues as alanine |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.474 |
| 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] | 54.233 | 2.160 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Number of reflections | 15690 | |
| <I/σ(I)> | 16.3 | 5.76 |
| Completeness [%] | 96.8 | 87.8 |
| Redundancy | 5 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Protein at 5mg/ml in 100mM NaCl, 25mM Tris pH 7.5. Crystals grew at and near 2M ammonium sulfate, 4% PEG400, 100mM NaAcetate pH5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
