6VTJ

Structure of a thiolation-reductase di-domain from an archaeal non-ribosomal peptide synthetase

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	2018-06-19
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9537
Spacegroup name	C 1 2 1
Unit cell lengths	98.949, 71.833, 82.725
Unit cell angles	90.00, 90.26, 90.00

Refinement procedure

Resolution	47.620 - 1.950
R-factor	0.198
Rwork	0.196
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4f6c
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.636	2.070
High resolution limit [Å]	1.948	1.950
Number of reflections	40262	4098
<I/σ(I)>	5.48
Completeness [%]	92.4
Redundancy	3.82
CC(1/2)	0.993	0.126

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.1	293.15	Crystals were grown by vapor diffusion, sitting drop method. Drop volume was 2 micro-liter (1+1) equilibrated against 50 micro-liter of reservoir volume of 1.7 M malic acid at pH 6.1. The concentration of protein was 30 mg/ml in HEPES buffer at pH 7.5 containing 150 mM of NaCl