6PAU

Structure of Human NMT2 with myristoyl-lysine peptide and CoA products

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	2019-03-21
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 1 21 1
Unit cell lengths	63.162, 46.350, 74.395
Unit cell angles	90.00, 114.25, 90.00

Refinement procedure

Resolution	67.831 - 1.930
R-factor	0.1984
Rwork	0.197
R-free	0.21770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4c2x
RMSD bond length	0.007
RMSD bond angle	0.877
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	57.590	1.999
High resolution limit [Å]	1.930	1.930
Rmerge	0.101	1.066
Rmeas	0.112
Number of reflections	154166	15911
<I/σ(I)>	11.35	1.54
Completeness [%]	99.5	99.56
Redundancy	5.2	5.3
CC(1/2)	0.998	0.646

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	8 mg/mL protein in a buffer of 25 mM Tris-HCl pH 7.5, 120 mM NaCl, 1 mM DTT, 1 mM MgCl2, mixed 1:1 with well solution of 22% PEG 8000, 0.1 M Bis-Tris pH 6.5