7KPF

NME2 bound to myristoyl-CoA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-10-11
Detector	DECTRIS PILATUS 300K
Wavelength(s)	0.97911
Spacegroup name	P 21 21 21
Unit cell lengths	84.727, 107.515, 115.080
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	78.560 - 2.230
Rwork	0.190
R-free	0.22910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3bbf
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.13-2998-0000)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	115.080	115.080	2.250
High resolution limit [Å]	2.180	9.260	2.180
Rmerge	0.103	0.030
Rmeas	0.111	0.033
Rpim	0.041	0.013
Total number of observations	375490	4981	13826
Number of reflections	52327	805	2139
<I/σ(I)>	13.2	46.2
Completeness [%]	94.7	96.8	47.6
Redundancy	7.2	6.2	6.5
CC(1/2)	0.998	0.998	0.597

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	The 2 mM NME2 protein (in 30 mM HEPES pH 8, 1 mM EDTA, 1 mM DTT) was mixed at a 1:1.1 ratio with 2 mM myristoyl-CoA in water and incubated on ice for 15 min. crystallized by vapor diffusion at 20 degrees C with a well solution of 10% PEG-4000, 100 mM MgCl2, 100 mM HEPES pH 7.5 and a protein-to-well drop ratio of 1:1