6B4A

Crystal structure of the C-Terminal Domain of Doublecortin (TgDCX) from Toxoplasma gondii ME49

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2017-08-03
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	36.860, 53.230, 96.380
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.725 - 2.000
R-factor	0.1935
Rwork	0.186
R-free	0.26070
Structure solution method	SAD
RMSD bond length	0.007
RMSD bond angle	0.784
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.7.17)
Refinement software	PHENIX (dev_2499)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.725	35.725	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.059	0.021	0.557
Rmeas	0.064	0.023	0.645
Number of reflections	13417	185	980
<I/σ(I)>	17.97	55.13	2.65
Completeness [%]	99.8	95.4	99.8
Redundancy	6.112	5.449	3.916
CC(1/2)	0.999	1.000	0.842

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	Rigaku Reagents PACT screen, optimized condition e6: 24.09% (w/v) PEG 3350, 50 mM sodium formate: TogoA.17199.a.B3.PW38274 at 15 mg/mL: cryo: 20% EG: tray 293956a11: puck utu4-1. For phasing, a crystal from Rigaku Reagents PACT screen condition e6 (18% (w/v) PEG 3350, 200 mM sodium formate) was soaked in reservoir plus 20% 2.5 M NaI in ethylene glycol and vitrified. Anomalous data was collected at the home source. Tray 292844e6: puck hly3-2.