8J2E

Structure of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus, mutant N940V/K1106W/S1114R 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	2019-11-11
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97876
Spacegroup name	C 1 2 1
Unit cell lengths	98.252, 128.020, 73.870
Unit cell angles	90.00, 103.38, 90.00

Refinement procedure

Resolution	31.040 - 2.120
R-factor	0.189
Rwork	0.188
R-free	0.21000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.010
Data reduction software	XDS (Mar 15, 2019 (BUILT 20190315))
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]	76.591	2.152
High resolution limit [Å]	2.116	2.116
Rmeas	0.058	0.699
Rpim	0.023	0.262
Number of reflections	50331	2487
<I/σ(I)>	16.7	2.2
Completeness [%]	99.5	100
Redundancy	6.5	7
CC(1/2)	0.999	0.886

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 (1 M sodium malonate pH 7.0).