8J2A

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

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	2019-01-09
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97849
Spacegroup name	C 1 2 1
Unit cell lengths	86.990, 139.940, 73.910
Unit cell angles	90.00, 98.61, 90.00

Refinement procedure

Resolution	24.890 - 1.700
R-factor	0.172
Rwork	0.171
R-free	0.19100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	0.940
Data reduction software	XDS (Jan 26, 2018, built on 20180409)
Data scaling software	Aimless (version 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]	69.968	1.726
High resolution limit [Å]	1.696	1.696
Rmeas	0.063	0.853
Rpim	0.024	0.320
Number of reflections	95052	4737
<I/σ(I)>	17	2.1
Completeness [%]	98.7	98.4
Redundancy	6.9	7
CC(1/2)	0.999	0.858

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The protein in complex with NADP+ was crystallized in drops containing 1.5 ul protein solution (15 mg/ml protein+2.6 mM NADP disodium salt, incubated at 4 degrees for 1 h) and 1.5 ul reservoir solution (100 mM HEPES pH 7.0, 20% w/v poly(acrylic acid sodium) 5100, 5 mM MgCl2)