5WHY

Structural Insights into Thioether Bond Formation in the Biosynthesis of Sactipeptides

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-11-16
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	1.0333
Spacegroup name	P 1
Unit cell lengths	51.929, 59.357, 81.363
Unit cell angles	83.09, 73.31, 66.63

Refinement procedure

Resolution	29.684 - 2.692
R-factor	0.2296
Rwork	0.225
R-free	0.28120
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5wgg
RMSD bond length	0.007
RMSD bond angle	0.950
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.000	30.000	2.750
High resolution limit [Å]	2.692	7.300	2.700
Rmerge	0.060	0.046	0.468
Rmeas	0.085	0.066	0.662
Rpim	0.060	0.046	0.468
Number of reflections	23072		1119
<I/σ(I)>	5.6
Completeness [%]	98.0	99.2	96.5
Redundancy	1.8	1.8	1.7
CC(1/2)		0.991	0.692

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	0.1M Tris-HCl, 0.2M calcium chloride, 25% polyethylene glycol 4,000