8TK6
HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE (VHR) in apo form
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 | 2023-04-16 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.97949 |
Spacegroup name | P 1 |
Unit cell lengths | 34.896, 41.283, 59.118 |
Unit cell angles | 86.58, 89.67, 75.06 |
Refinement procedure
Resolution | 59.010 - 1.650 |
R-factor | 0.14773 |
Rwork | 0.146 |
R-free | 0.18336 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.581 |
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] | 59.010 | 1.730 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.037 | 0.078 |
Number of reflections | 32373 | 2000 |
<I/σ(I)> | 12.8 | 9.85 |
Completeness [%] | 88.7 | 51 |
Redundancy | 1.8 |
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, 28% (w/v) PEG-4000) and equilibrated against the precipitant solution. |