6AWL

Crystal structure of human Coq9

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-02-07
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0332
Spacegroup name	P 1 21 1
Unit cell lengths	38.110, 97.390, 63.650
Unit cell angles	90.00, 95.40, 90.00

Refinement procedure

Resolution	48.690 - 2.000
R-factor	0.2003
Rwork	0.197
R-free	0.24540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4rhp
RMSD bond length	0.003
RMSD bond angle	0.661
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.690	2.071
High resolution limit [Å]	2.000	2.000
Rmerge	0.091	1.355
Rpim	0.044	0.658
Number of reflections	31242	3066
<I/σ(I)>	12.38	1.25
Completeness [%]	100.0	99.9
Redundancy	5.1	5.1
CC(1/2)	0.998	0.480

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Protein was dissolved at 4.89 mg/mL in a buffer containing 10 mM HEPES pH 7.5, 100 mM NaCl, 0.3 mM TCEP. 200 nL of protein was mixed with 200 nL of reservoir in a SD2 plate. The reservoir consisted of 21% w/v PEG 3350, 0.25 M NaCl, and 0.1 M bistris pH 6.5. Crystals were cryopreserved in 35% PEG 3350, 0.2 M NaCl and 0.1 M bistris buffer, pH 6.5.