8TK3

HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE (VHR) having oxidized catalytic cysteine and complexed with 6-(difluoromethyl)pyrimidin-4-ol at two allosteric sites

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-02-17
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.9201
Spacegroup name	P 21 21 21
Unit cell lengths	34.133, 52.467, 100.493
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.250 - 2.000
R-factor	0.18968
Rwork	0.186
R-free	0.25538
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.593
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0411)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.300	2.180
High resolution limit [Å]	1.950	1.950
Rmerge	0.130	0.680
Number of reflections	13585	3842
<I/σ(I)>	7.8	2.7
Completeness [%]	99.0	96.1
Redundancy	6.4	7
CC(1/2)	0.990	0.910

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	The protein in 50 mM TRIS-Cl pH 8.5, 1 mM TCEP, 0.5 mM EDTA was mixed with the crystallization buffer (100 mM Bis-Tris pH 6.5, 50 mM NH4F, 28% (w/v) PEGME-2000) and equilibrated against the crystallization buffer. The crystals were soaked with 25 mM of the compound in solution (10% DMSO, 100 mM Bis-Tris pH 6.5, 50 mM NH4F, 28% (w/v) PEGME-2000).