5KQT
Directed Evolution of Transaminases By Ancestral Reconstruction. Using Old Proteins for New Chemistries
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-05-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 66.346, 66.346, 343.314 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.800 - 1.990 |
| R-factor | 0.19778 |
| Rwork | 0.196 |
| R-free | 0.23695 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gju |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.389 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.800 | 2.100 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.136 | 0.720 |
| Number of reflections | 32214 | |
| <I/σ(I)> | 17.6 | 4.9 |
| Completeness [%] | 99.9 | 99.3 |
| Redundancy | 20.7 | 20.7 |
| CC(1/2) | 0.998 | 0.910 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 293 | 150 nL plus 150 nL drops of protein at 5 mg/mL and reservoir which consisted of 1.6 M ammonium sulfate, 1% dioxane, 50 mM MES pH 6.8 |
