6C6G

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex.

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	2017-07-06
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.95370
Spacegroup name	I 1 2 1
Unit cell lengths	78.629, 88.909, 141.852
Unit cell angles	90.00, 101.32, 90.00

Refinement procedure

Resolution	74.910 - 2.100
R-factor	0.16858
Rwork	0.166
R-free	0.20952
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ip4 and 3dha
RMSD bond length	0.014
RMSD bond angle	1.639
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]	74.910	2.160
High resolution limit [Å]	2.100	2.100
Rmerge	0.326	1.282
Rpim	0.126	0.496
Number of reflections	55955	4588
<I/σ(I)>	6.7
Completeness [%]	100.0	100
Redundancy	7.6	7.6
CC(1/2)	0.982	0.656

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	100 mM bis-tris at pH 5.5, 128 mM MgCl2, 21% (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 20 C.