5V0W

Crystal structure of glycylpeptide N-tetradecanoyltransferase from Plasmodium vivax in complex with inhibitor IMP-0001088

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	57.320, 119.130, 176.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.575 - 1.800
R-factor	0.1473
Rwork	0.147
R-free	0.18400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4b14
RMSD bond length	0.007
RMSD bond angle	0.935
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]	50.000	50.000	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.107	0.036	0.515
Rmeas	0.115	0.039	0.562
Number of reflections	112736	1415	8213
<I/σ(I)>	15.21	37.67	3.74
Completeness [%]	99.9	99.4	99.4
Redundancy	7.248	6.611	6.268
CC(1/2)	0.998	0.999	0.905

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	27% PEG 3350, 200 mM Ammonium Sulfate, 100 mM BisTris pH 6.0, 0.5mM IMP-0001088, 0.5mM myristoyl CoA; protein conc 12.53mg/mL; hdg0-9