5KQW
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 | 66.051, 125.179, 110.496 |
Unit cell angles | 90.00, 101.97, 90.00 |
Refinement procedure
Resolution | 47.200 - 2.230 |
R-factor | 0.16514 |
Rwork | 0.164 |
R-free | 0.19198 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5kqt |
RMSD bond length | 0.013 |
RMSD bond angle | 1.560 |
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] | 47.200 | 2.270 |
High resolution limit [Å] | 2.230 | 2.230 |
Rmerge | 0.130 | 0.739 |
Number of reflections | 85391 | |
<I/σ(I)> | 9.2 | 2.3 |
Completeness [%] | 99.8 | 99.1 |
Redundancy | 3.8 | 3.6 |
CC(1/2) | 0.988 | 0.654 |
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 15% PEG 8000, 17% glycerol, 150 mM MgCl2, 100 mM Tris pH 7.2. Seeding used to nucleate crystal formation. |