We continued solution scattering measurements of the wild-type and mutant P22 capsid. Instrument calibration was done more carefully this time than last year, and we observed scattering peaks whose Bragg spacing match very well with those calculated from the EM structures that the Baylor group had obtained. In the higher angle region, we have a few characteristic peaks that may arise from b-sheet structure of the capsid protein and/or from RNA packing inside. We measured solution x-ray scattering from the scaffolding protein in the temperature range 15 - 60 !C. Clear changes in the assembly state of the scaffolding protein were seen in subsidiary scattering peaks. The studies were continued on a separate experimental proposal by W. Chiu et al.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-19
Application #
2788409
Study Section
Project Start
Project End
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
19
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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