7RK3

Crystal structure of human N-myristoyltransferase 1 fragment (residues 109-496) bound to diacylated human Arf6 octapeptide and Coenzyme A

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	2019-11-26
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 21 21 21
Unit cell lengths	47.984, 76.046, 106.342
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	61.860 - 2.050
R-factor	0.1616
Rwork	0.159
R-free	0.21970
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	HsNMT1
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHENIX (1.19.1_4122)
Refinement software	PHENIX (1.19.1_4122)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	106.340	106.340	2.110
High resolution limit [Å]	2.050	8.930	2.050
Rmerge	0.066	0.015	0.475
Rmeas	0.078	0.018	0.571
Rpim	0.040	0.010	0.310
Total number of observations	88647	1201	5739
Number of reflections	24871	375	1833
<I/σ(I)>	13.1	43.8	2.1
Completeness [%]	99.0	99.9	96.1
Redundancy	3.6	3.2	3.1
CC(1/2)	0.998	1.000	0.860

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		295	20% (w/v) PEG 3350, 200mM ammonium formate