A comparison between the crystal and solution structures of Escherichia coli asparaginase II. | Zendy

Maciej Kozak | Zendy; Stefan Jurga | Zendy

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A comparison between the crystal and solution structures of Escherichia coli asparaginase II.

Author(s) -

Maciej Kozak,

Stefan Jurga

Publication year - 2002

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2002_3810

Subject(s) - small angle x ray scattering , radius of gyration , crystal (programming language) , crystallography , crystal structure , chemistry , escherichia coli , radius , homotetramer , scattering , materials science , physics , optics , polymer , biochemistry , organic chemistry , computer security , protein subunit , computer science , gene , programming language

The small angle X-ray scattering (SAXS) pattern of the homotetrameric asparaginase II from Escherichia coli was measured in solution in conditions resembling those in which its crystal form was obtained and compared with that calculated from the crystallographic model. The radius of gyration measured by SAXS is about 5% larger and the maximum dimension in the distance distribution function about 12% larger than the corresponding value calculated from the crystal structure. A comparison of the experimental and calculated distance distribution functions suggests that the overall quaternary structure in the crystal and in solution are similar but that the homotetramer is less compact in solution than in the crystal.

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