8J2B

Structure of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus, in complex with NADP+ and malonate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-11-18
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97906
Spacegroup name	C 1 2 1
Unit cell lengths	100.960, 125.220, 73.810
Unit cell angles	90.00, 105.59, 90.00

Refinement procedure

Resolution	62.610 - 2.130
R-factor	0.186
Rwork	0.185
R-free	0.20300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.050
Data reduction software	XDS (Jan 26, 2018 (BUILT 20180409))
Data scaling software	Aimless (0.5.29)
Phasing software	PHASER (2.7.17)
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	62.612	2.163
High resolution limit [Å]	2.127	2.127
Rmeas	0.060	0.784
Rpim	0.023	0.289
Number of reflections	48013	2428
<I/σ(I)>	17.7	2.3
Completeness [%]	96.9	97.5
Redundancy	6.7	7.3
CC(1/2)	0.999	0.793

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The protein in complex with NADP+ and malonate was obtained by crystallizing in drops containing 1.5 ul protein solution (10 mg/ml protein+1.7 mM NADP disodium salt, incubated at 4 degrees for 1 h) and 1.5 ul reservoir solution (250 mM sodium malonate pH 7.0, 10% w/v PEG 6000).