9DJ9

HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE (VHR) in distinct apo form

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	2024-02-11
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.92010
Spacegroup name	P 1 21 1
Unit cell lengths	35.227, 59.204, 43.195
Unit cell angles	90.00, 102.84, 90.00

Refinement procedure

Resolution	34.318 - 1.924
R-factor	0.1922
Rwork	0.190
R-free	0.23860
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	autoPROC (1.0.5)
Data scaling software	Aimless (0.7.7)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.318	1.958
High resolution limit [Å]	1.924	1.924
Rmerge	0.135	1.561
Rmeas	0.163	1.884
Rpim	0.091	1.042
Number of reflections	12987	656
<I/σ(I)>	5.7	0.8
Completeness [%]	98.2	98.8
Redundancy	3	3.1
CC(1/2)	0.994	0.341

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	Protein in 50 mM TRIS-Cl pH 8.5, 1 mM TCEP, 0.5 mM EDTA was mixed with the precipitant solution (100 mM Bis-Tris pH 6.5, 50 mM NH4F, 26.7% (w/v) PEG-4000) and equilibrated against the precipitant solution.