5KQU
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 | 2014-03-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.104, 146.886, 131.776 |
| Unit cell angles | 90.00, 97.68, 90.00 |
Refinement procedure
| Resolution | 48.900 - 2.620 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5kqt |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.504 |
| 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] | 48.900 | 2.670 |
| High resolution limit [Å] | 2.620 | 2.620 |
| Rmerge | 0.138 | 0.742 |
| Number of reflections | 83580 | |
| <I/σ(I)> | 11.3 | 2.5 |
| Completeness [%] | 99.7 | 95.1 |
| Redundancy | 7.5 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 150 plus 150 nL drops with protein at 10 mg/mL and a reservoir of 15% PEG 8000, 13% glycerol, 155 mM MgCl2, 100 mM Tris pH 8.5 |
