Crystallization and preliminary X-ray diffraction studies of Theiler's virus (GDVII strain)
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K S Toth1, C X Zhang, H L Lipton
1Department of Microbiology, University of Alabama, Birmingham 35294.
Abstract:
Theiler's murine encephalomyelitis virus (TMEV) is a member of the picornavirus family. Mice infected with TMEV serve as models for the study of human neurological diseases including multiple sclerosis. Preparations of the GDVII strain of Theiler's virus have been crystallized using the hanging drop technique. When exposed to high intensity synchrotron radiation, these monoclinic crystals diffracted X-rays to at least 3.0 A resolution. The unit cell has a C-centered lattice with dimensions: a = 575.2 A, b = 324.0 A and c = 558.4 A, beta = 108.2 degrees. The molecular mass and cell dimensions imply that there is an entire virus particle per asymmetric unit, suggesting the presence of 60-fold non-crystallographic redundancy. This GDVII crystal form appears to be suitable for high-resolution structure determination.
Insights
Theiler's murine encephalomyelitis virus (TMEV) GDVII strain was crystallized. These crystals diffracted X-rays, enabling high-resolution structural analysis for neurological disease research.
Area of Science:
- Virology
- Structural Biology
- Neuroscience
Background:
- Theiler's murine encephalomyelitis virus (TMEV) is a picornavirus.
- TMEV-infected mice are models for human neurological diseases like multiple sclerosis.
Purpose of the Study:
- To crystallize the GDVII strain of TMEV.
- To assess the suitability of GDVII crystals for high-resolution structure determination.
Main Methods:
- Hanging drop technique for TMEV crystallization.
- Synchrotron X-ray diffraction analysis of crystals.
Main Results:
- Monoclinic crystals of GDVII strain TMEV were successfully prepared.
- Crystals diffracted X-rays to at least 3.0 A resolution.
- Unit cell dimensions and molecular mass suggest one virus particle per asymmetric unit with 60-fold non-crystallographic redundancy.
Conclusions:
- The GDVII crystal form is suitable for high-resolution structure determination.
- This facilitates understanding TMEV structure and its role in neurological diseases.