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] | 50.250 | 1.810 |
High resolution limit [Å] | 1.780 | 1.780 |
Rmerge | 0.170 | |
Number of reflections | 17972 | 1234 |
<I/σ(I)> | 5 | |
Completeness [%] | 99.3 | 96.1 |
Redundancy | 6.4 | 4 |
CC(1/2) | 0.990 | 0.370 |
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). |