Complementarity of Neutron and Ultrahigh Resolution Synchrotron X-Ray Protein Crystallography Studies: Results with Concanavalin A at Cryo and Room Temperature
Year: 2002
Type: article
Abstract: t ment of Chem i str y, Uni versi ty of Ma n chester, M 13 9P L, U K T h e c om plement ar it y of synchrotron deri ved ultrahi gh resolution X -ray and neutron protein crystallograp hy is explored via an ensem ble of plant lectin concana valin A crystal structures .T hus a resume of a study of a cryo 0.94 ¡ A and a neutron (+ X -ray ) protein crystal 2.4 ¡ A structure at ro om temp erature is made and these are then compared in their e£ciency to determine the positio ns of the bound solvent atoms i. e. as hydrogens or deuteriums.First results are also presented of comparisons of t w o ultrahigh resolutio n protein crystal structures , the 0. 94 ¡ A and a new 0. 92 ¡ A structure.T hus the v ariabili ty of the tw o cryo structures, at very Ùne detail, is describ ed; this v ariabili ty is in the multiple occupancies of side chains.Overall, one can see that a \complete " structure deÙniti on, w ith to day ' s exp erimental capabilities, is possibl e and can inclu de structure ensemble v ariations.PAC S numb ers: 87.64.
Source: Acta Physica Polonica A
Institution: University of Manchester
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: diamond
OpenAlex ID: W1505569029