6KIN

Crystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholzii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U1
Synchrotron site	SSRF
Beamline	BL17U1
Temperature [K]	100
Detector technology	CCD
Collection date	2018-07-18
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97893
Spacegroup name	P 21 21 21
Unit cell lengths	122.033, 133.417, 139.595
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.225 - 2.527
R-factor	0.1784
Rwork	0.176
R-free	0.23370
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4l7z
RMSD bond length	0.008
RMSD bond angle	0.926
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	PHENIX (1.11.1_2575)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.097	0.387
Rpim	0.047	0.186
Number of reflections	73219	3642
<I/σ(I)>	7.3
Completeness [%]	96.6	97.9
Redundancy	4.6
CC(1/2)	0.987	0.905

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289	The protein sample was mixed with an equal volume of the reservoir solution (16 % (v/v) PEG3350 and 0.2 M sodium chloride), and the mixture was equilibrated against the reservoir solution.