5KC1

Structure of the C-terminal dimerization domain of Atg38

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2014-09-29
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.976260
Spacegroup name	P 21 21 2
Unit cell lengths	81.383, 249.385, 50.197
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	58.000 - 2.200
R-factor	0.2064
Rwork	0.205
R-free	0.24060
Structure solution method	MAD
RMSD bond length	0.005
RMSD bond angle	0.769
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	autoSHARP
Refinement software	PHENIX (dev_1810)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	58.100	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.062	0.891
Number of reflections	52821
<I/σ(I)>	16.9	2.3
Completeness [%]	99.8	99.6
Redundancy	6.6	6.3
CC(1/2)	0.999

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	290	1.97 M ammonium nitrate, 0.15 M (D/L) malate pH 5.0 and 0.136 M Mg sulfate The full-length Atg38 protein was subjected to limited proteolysis. Atg38 (300 microliters at 16 mg/mL in gel-filtration buffer containing 20 mM Tris-HCl pH 8.8, 150 mM NaCl, 1 mM TCEP) was mixed with subtilisin (3 microliters at 1 mg/mL, using subtilisn from the ProteAce kit, Hampton Research), incubated for 10 h at 4 degrees C and set up for crystallization without further purification