6OD8

Crystal structure of a putative aspartyl-tRNA synthetase from Leishmania major Friedlin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2019-03-08
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	61.010, 142.360, 68.280
Unit cell angles	90.00, 97.20, 90.00

Refinement procedure

Resolution	46.111 - 1.850
R-factor	0.1574
Rwork	0.157
R-free	0.19190
Structure solution method	SAD
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.15rc1_3423))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.111	46.111	1.900
High resolution limit [Å]	1.850	8.270	1.850
Rmerge	0.061	0.031	0.334
Rmeas	0.064	0.032	0.400
Total number of observations	851909
Number of reflections	97249	1127	6661
<I/σ(I)>	20.88	51.15	2.87
Completeness [%]	99.0	99.1	92.1
Redundancy	8.76	10.97	3.109
CC(1/2)	0.999	0.999	0.872

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Microlytic MCSG-1 screen G9: 20% (w/V) PEG 3350, 200mM sodium formate: LemaA.00612.a.B1.PW38547 at 21.8mg/ml: cryo: 20% EG in two steps: tray 306454 G9: puck xyn7-2. For experimental phasing, a crystal from the same well was incubated for 10sec each in a solution of a) 90% reservoir and 10% 2.5M Sodium iodide in ethylene glycol and a solution of b) a) 80% reservoir and 20% 2.5M Sodium iodide in ethylene glycol a s and vitrified: puck: bbh6-4. Well diffracting monoclinic crystals with a larger unit cell and four copies of the protein in the ASU also grew under condition MCSG-1 D9: 25% (w/V) PEG 3350, 200mM NaCl, 100mM Tris pH 8.5