6VTZ

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	2017-07-19
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.953
Spacegroup name	P 32 2 1
Unit cell lengths	139.920, 139.920, 71.750
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.291 - 2.650
R-factor	0.2051
Rwork	0.203
R-free	0.24560
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]	46.291	2.830
High resolution limit [Å]	2.650	2.650
Rmeas	0.221
Number of reflections	23800	8693
<I/σ(I)>	7.07
Completeness [%]	99.9
Redundancy	10.72
CC(1/2)	0.996	0.338

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293.15	Crystals were grown by vapour diffusion, hanging drop method. Drop volume was 2 micro-litre (1+1) equilibrated against 500 micro-litre of reservoir volume containing 0.1 M MOPS/Na-HEPES buffer at pH 7.5, 15% PEG MME and 14% PEG 20K as precipitants in the presence of 0.02M each of L-Na Glutamate, DL-Alanine, Glycine, DL-Lysine HCl, DL-Serine as additives. The concentration of protein was 30 mg/ml in HEPES buffer at pH 7.5 containing 150 mM NaCl