8FBU

Crystal structure of Cryptosporidium parvum N-myristoyltransferase with bound myristoyl-CoA and Compound-2

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.1
Synchrotron site	ALS
Beamline	8.2.1
Temperature [K]	100
Detector technology	CCD
Collection date	2019-05-01
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0000
Spacegroup name	P 1 21 1
Unit cell lengths	53.777, 88.228, 98.060
Unit cell angles	90.00, 97.83, 90.00

Refinement procedure

Resolution	35.370 - 2.000
R-factor	0.1577
Rwork	0.155
R-free	0.20670
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.122
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	PHENIX (1.20.1.4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.030
High resolution limit [Å]	2.000	2.000
Rmeas	0.109	0.927
Rpim	0.058	0.506
Number of reflections	59810	2994
<I/σ(I)>	14.3	1.46
Completeness [%]	97.5	99
Redundancy	3.3	3.3
CC(1/2)	0.990	0.504

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	CrpaA.18219.a.A10.PS38408 at 17.5 mg/mL was incubated with final concentrations of 0.8 mM Myristoyl-CoA and 1.0 mM compound at 4C for 30 min, then mixed with 1:1 with 100 mM BisTris-HCl pH 6.5 and 27.5% PEG 3350. Protein buffer is 25 mM HEPES pH 7.0, 500 mM NaCl, 5% Glycerol, 2 mM DTT, 0.025% Azide. Crystals are harvested using crystallant plus 25% PEG 400