The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-ray Diffraction
β Scribed by Coates, Leighton; Tuan, Han-Fang; Tomanicek, Stephen; Kovalevsky, Andrey; Mustyakimov, Marat; Erskine, Peter; Cooper, Jon
- Book ID
- 120570807
- Publisher
- American Chemical Society
- Year
- 2008
- Tongue
- English
- Weight
- 613 KB
- Volume
- 130
- Category
- Article
- ISSN
- 0002-7863
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Statistical mcchanicdl models are frequently used m the interpretation of X-ray and neutron diffraction data from molccular liquids and mixtures, where it is not possible to obtain complete structural information by Fourier inversion. Such modclling procedures arc tested here by comparing the pair c
## Abstract Recombinant human adenovirus serotype 2 proteinase (both native and selenomethionineβsubstituted) has been crystallized in the presence of the serotype 12, 11βresidue peptide cofactor. The crystals (space group P3~1~21 or P3~2~21, one molecule per asymmetric unit, __a = b__ = 41.3 Γ , __