7XYK

Structure of WSSV thymidylate synthase in complex with dUMP and raltitrexed

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL19U1
Synchrotron site	SSRF
Beamline	BL19U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-06-01
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97853
Spacegroup name	P 1 21 1
Unit cell lengths	51.164, 90.113, 123.996
Unit cell angles	90.00, 92.98, 90.00

Refinement procedure

Resolution	51.100 - 1.433
R-factor	0.1487
Rwork	0.148
R-free	0.16960
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6k7r
RMSD bond length	0.009
RMSD bond angle	1.129
Data reduction software	XDS (Jan 26, 2018, built on 20180409)
Data scaling software	Aimless (version 0.5.29)
Phasing software	PHASER (2.7.17)
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	72.862	1.437
High resolution limit [Å]	1.433	1.433
Rmeas	0.053	0.891
Rpim	0.020	0.332
Number of reflections	203509	2000
<I/σ(I)>	17.5	2
Completeness [%]	98.9	98.5
Redundancy	6.8	7
CC(1/2)	0.999	0.803

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The protein in complex with dUMP and raltitrexed was crystallized in drops containing 1 ul protein solution (10 mg/ml protein + 5 mM dUMP + 5 mM raltitrexed incubated at 4 degrees for 4 h) and 1 ul reservoir solution (100 mM Bis-Tris pH 6.5, 25% (w/v) PEG 3350, 200 mM (NH4)2SO4), and the cryo-buffer was 100 mM Bis-Tris pH 6.5, 35% (w/v) PEG 3350, 200 mM (NH4)2SO4.