38LL

Crystal Structure of serine/threonine-protein kinase (AEK1) from Trypanosoma brucei (hesperidin)

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	2026-06-13
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	I 2 2 2
Unit cell lengths	86.160, 88.940, 200.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	79.150 - 2.650
R-factor	0.2224
Rwork	0.220
R-free	0.26960
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.785
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((2.2_6163: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	81.284	2.747
High resolution limit [Å]	2.650	2.650
Rmerge	0.148	1.678
Rmeas	0.160	1.807
Rpim	0.060	0.667
Number of reflections	18123	906
<I/σ(I)>	13.6	1.7
Completeness [%]	79.5	39.7
Redundancy	13.2	13.6
CC(1/2)	0.998	0.638

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291	Index A3: 0.1M Bis-Tris pH 5.5, 2.0M Ammonium Sulfate. TrbrA.01480.a.WW4.PS38793 at 13.5 mg/mL. The C-terminal tail ~60 residues was disordered in each subunit. 24h soak in 2mM hesparidin in crystallant. plate BK6-pg64Clover-C3, IDX A3, Puck: PSL-0304, Cryo: 2.5M Li2SO4. Anisotropically truncated data were used for refinement.