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.