8J2C

Structure of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus, mutant N940V/K1106W/S1114R

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	2017-06-23
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97774
Spacegroup name	C 1 2 1
Unit cell lengths	89.273, 133.029, 74.119
Unit cell angles	90.00, 100.50, 90.00

Refinement procedure

Resolution	73.265 - 1.700
R-factor	0.17
Rwork	0.169
R-free	0.18800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	0.930
Data reduction software	XDS (version (Nov 1, 2016, built on 20170215)
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]	73.265	1.702
High resolution limit [Å]	1.697	1.697
Rmeas	0.063	0.674
Rpim	0.024	0.277
Number of reflections	91959	734
<I/σ(I)>	17.3	2.2
Completeness [%]	98.2	76.1
Redundancy	6.7	5.7
CC(1/2)	0.999	0.815

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The protein was crystallized in drops containing 1.5 ul protein solution (5 mg/ml) and 1.5 ul reservoir solution (1.1 M ammonium tartrate pH 7.0)