8J2D

Structure of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus, mutant N940V/K1106W/S1114R 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	2019-11-11
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97876
Spacegroup name	C 1 2 1
Unit cell lengths	97.220, 126.010, 73.440
Unit cell angles	90.00, 102.33, 90.00

Refinement procedure

Resolution	32.360 - 2.210
R-factor	0.195
Rwork	0.193
R-free	0.22700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.070
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]	75.846	2.243
High resolution limit [Å]	2.205	2.205
Rmeas	0.084	0.847
Rpim	0.032	0.318
Number of reflections	43280	2146
<I/σ(I)>	13.6	2.1
Completeness [%]	99.5	100
Redundancy	6.7	7
CC(1/2)	0.999	0.841

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 (10 mg/ml protein+1.7 mM NADP disodium salt, incubated at 4 degrees for 1 h) and 1.5 ul reservoir solution (100 mM sodium citrate pH 5.0, 150 mM sodium citrate, 16% w/v PEG3350).