6DEW

Structure of human COQ9 protein with bound isoprene.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-11-19
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.127230
Spacegroup name	C 2 2 21
Unit cell lengths	116.450, 222.780, 130.780
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.000 - 2.000
R-factor	0.17
Rwork	0.169
R-free	0.20940
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6awl
RMSD bond length	0.019
RMSD bond angle	1.357
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.127	1.759
Rmeas	0.133	1.824
Rpim	0.036	0.480
Number of reflections	114146	11326
<I/σ(I)>	15.48	1.51
Completeness [%]	99.7	99.87
Redundancy	13.5	14.1
CC(1/2)	0.998	0.622

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	8.5	293	Crystals were grown by seeded micro batch in a glass depression plate, on glass coverslips. The experiment was sealed with FOMBLIN oil. 2 microliters of protein saturated with geranylgeraniol was mixed with 1 microliter of seed stock and two microliters of reservoir solution. The reservoir solution was composed of 1.2 molar ammonium sulfate and 0.1 molar TrisHCl buffer at pH 8.5. The reservoir was saturated with geranylgeraniol by adding several microliters of neat geranylgeraniol.