9YRU

Crystal structure of Apo Cysteinyl-tRNA synthetase (CysRS) from Plasmodium falciparum (Orthrhombic P form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2025-07-26
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 21 21 21
Unit cell lengths	63.874, 104.024, 158.805
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.770 - 3.060
R-factor	0.2315
Rwork	0.229
R-free	0.28760
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.791
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((2.0_5765: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.770	3.140
High resolution limit [Å]	3.060	3.060
Rmerge	0.109	2.163
Rmeas	0.114	2.249
Rpim	0.031	0.611
Total number of observations	270129	19643
Number of reflections	20666	1464
<I/σ(I)>	16.7	1.4
Completeness [%]	99.9
Redundancy	13.1	13.4
CC(1/2)	0.999	0.767

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.9	291	Berkeley D7: 100mM potassium phosphate dibasic, 100 mM potassium chloride, 30% PEG 3350. PlfaA.00133.a.A3.PS38777 at 12.3 mg/mL. 4mM ATP added to the protein prior to screening but ligand is not bound likely due to high phosphate concentration in the crystallant. plate 20147 D7 drop 1 , Puck: PSL-0309, Cryo: direct