8J29

Structures of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus

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	2016-11-17
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97852
Spacegroup name	C 1 2 1
Unit cell lengths	86.410, 139.460, 73.870
Unit cell angles	90.00, 98.24, 90.00

Refinement procedure

Resolution	27.530 - 1.880
R-factor	0.177
Rwork	0.176
R-free	0.20100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	0.950
Data reduction software	XDS (Jan 26, 2018, built on 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]	72.902	1.883
High resolution limit [Å]	1.877	1.877
Rmeas	0.056	0.760
Rpim	0.021	0.282
Number of reflections	68842	657
<I/σ(I)>	21.9	2.3
Completeness [%]	97.7	97.9
Redundancy	7	7.1
CC(1/2)	1.000	0.877

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 (10 mg/ml) and 1.5 ul reservoir solution (900 mM ammonium tartrate pH 6.0)