8EW8

Crystal structure of Saccharomyces cerevisiae Altered Inheritance rate of Mitochondria protein 18 (AIM18p) R123A mutant

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-02-07
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.964370, 0.979370, 0.979610
Spacegroup name	P 32 2 1
Unit cell lengths	127.390, 127.390, 54.270
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	48.700 - 2.150
R-factor	0.1808
Rwork	0.178
R-free	0.21160
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	0.798
Data reduction software	XDS (VERSION Nov 11, 2017 BUILT=20171111)
Data scaling software	XSCALE (VERSION Nov 11, 2017 BUILT=20171111)
Phasing software	PHASER (2.8.0)
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.700	2.227
High resolution limit [Å]	2.150	2.150
Rmerge	0.098	0.996
Rmeas	0.101	1.039
Rpim	0.023	0.284
Number of reflections	27153	2241
<I/σ(I)>	21.8	2.38
Completeness [%]	97.6	81.11
Redundancy	18.8	12.3
CC(1/2)	0.999	0.702

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	Crystals for data collection were obtained by mixing 200 nL of protein soiution (15.1 mg/mL Nd70 R123A Aim18p, 20 mM HEPES buffer, pH 7.5, 200 mM NaCl, 2 mM TCEP) with 150 nL of reservoir solution (26% PEG 3350, 200 mM Li2SO4, 100 mM HEPES pH 7.5) in a SD2 crystallization tray with a TTP Labtech Mosquito crystallization robot. Crystals were cryoprotected with reservoir solution supplemented to 30% PEG 3350