5V0X

Crystal structure of glycylpeptide N-tetradecanoyltransferase from Plasmodium vivax in complex with inhibitor IMP-0001114

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2017-01-27
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97949
Spacegroup name	P 21 21 21
Unit cell lengths	57.200, 118.010, 173.710
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.808 - 2.100
R-factor	0.1643
Rwork	0.163
R-free	0.22120
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4b14
RMSD bond length	0.007
RMSD bond angle	0.909
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.808	50.000	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.128	0.029	0.447
Rmeas	0.148	0.034	0.519
Number of reflections	69068	872	4904
<I/σ(I)>	11.25	31.36	3.74
Completeness [%]	99.3	97.5	97
Redundancy	4.103	3.665	3.873
CC(1/2)	0.992	0.999	0.824

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	22% PEG 3350, 200 mM Ammonium Sulfate, 100 mM BisTris pH 5.5, 0.5mM IMP-0001114, 0.5mM myristoyl CoA: protein conc 12.53mg/mL: hdg0-1