5KR6
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 315r |
Wavelength(s) | 0.95370 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.088, 123.240, 63.251 |
Unit cell angles | 90.00, 117.61, 90.00 |
Refinement procedure
Resolution | 48.800 - 1.990 |
R-factor | 0.19753 |
Rwork | 0.195 |
R-free | 0.23929 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kqt |
RMSD bond length | 0.013 |
RMSD bond angle | 1.553 |
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] | 48.800 | 2.040 |
High resolution limit [Å] | 1.990 | 1.990 |
Rmerge | 0.075 | 0.320 |
Number of reflections | 55970 | |
<I/σ(I)> | 13 | 3.4 |
Completeness [%] | 98.5 | 98.1 |
Redundancy | 3.7 | 3.6 |
CC(1/2) | 0.995 | 0.859 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 150 plus 150 nL drops with protein at 10 mg/mL and reservoir conditions of 16% PEG 3350, 215 mM ammonium formate. Microseeds were used to produce full size crystals. |