6NE6

Crystal Structure of heterotrimeric G-protein alpha subunit Galpha7 from Naegleria fowleri

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2018-04-05
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	60.690, 68.310, 79.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.256 - 1.700
R-factor	0.163
Rwork	0.161
R-free	0.19470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5do9
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.256	48.256	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.046	0.022	0.512
Rmeas	0.050	0.025	0.572
Total number of observations	222267
Number of reflections	37029	458	2695
<I/σ(I)>	23.09	58.88	2.99
Completeness [%]	99.8	96.2	99.8
Redundancy	6.003	5.238	4.996
CC(1/2)	0.999	0.999	0.858

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	NafoA.01088.e.B1 and NafoA.19531.b.B2 were co-purified (PW38434) to 20.24 mg/ml in a buffer containing 25 mM HEPES pH 7.5, 500 mM NaCl, 5% Glycerol , 2 mM DTT, 0.025% Azide, 10mM MgCl2, 10mM NaF, 30uM AlCl3, 5uM GDP, was mixed 1:1 with Wiz3/4(c8): 16% (w/v) PEG-800, 40 mM potassium phosphate monobasic, 20% (v/v) glycerol, cryoprotected with 20% ethylene glycol. Tray 299259c8, puck: rhn8-4