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X‐ray Scattering Studies of Metalloproteins in Solution: a Quantitative Approach for Studying Molecular Conformations, a Quantitative Approach for Studying Molecular Conformations.
Author(s) -
Günter Grossmann J.,
Hasnain S. S.
Publication year - 1997
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889897001581
Subject(s) - multipole expansion , chemistry , metalloprotein , scattering , computational chemistry , synchrotron , crystallography , chemical physics , physics , optics , enzyme , organic chemistry , quantum mechanics
The model‐independent approach based on the multipole expansion method using spherical harmonics [Stuhrmann (1970 a ). Acta Cryst. A 26 , 297–306] has been applied to obtain structural information on a variety of metalloproteins studied by synchrotron X‐ray solution scattering. The method is applied to examples (nitrite reductase, transferrin and nitrogenase), not only with the view of comparing protein conformations in solution with those in the crystalline state, but also defining conformational changes and protein‐protein interactions which are of functional importance. The shape restoration is found to be straightforward at low resolution ( L ≤ 3). For correct treatment using higher harmonics, overall molecular symmetry, if present, must be included in the multipole expansion.