6C62
An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
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 | PIXEL |
Collection date | 2017-07-15 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.99989 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 79.489, 89.040, 141.672 |
Unit cell angles | 90.00, 101.89, 90.00 |
Refinement procedure
Resolution | 69.300 - 1.950 |
R-factor | 0.15478 |
Rwork | 0.153 |
R-free | 0.19066 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ip4 and 3dha |
RMSD bond length | 0.017 |
RMSD bond angle | 1.726 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | MoRDa |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 69.300 | 1.990 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.233 | 1.545 |
Rpim | 0.095 | 0.622 |
Number of reflections | 70426 | 4504 |
<I/σ(I)> | 6.9 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.9 | 7.1 |
CC(1/2) | 0.991 | 0.804 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 281 | 100mM bis-tris at pH 6.0, 276 mM MgCl2, 17.6 (w/v) PEG 8000 in the reservoir with protein at 1.1 mg/mL with 0.05% agarose gel in 250 plus 250 nL drops at 8 C. |