Structure and growth of ultrasmall protein microcrystals by synchrotron radiation: I. µGISAXS and µdiffraction of P450scc | Zendy

Nicolini Claudio | Zendy; Pechkova Eugenia | Zendy

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Structure and growth of ultrasmall protein microcrystals by synchrotron radiation: I. µGISAXS and µdiffraction of P450scc

Author(s) -

Nicolini Claudio,

Pechkova Eugenia

Publication year - 2005

Publication title -

journal of cellular biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.028

H-Index - 165

eISSN - 1097-4644

pISSN - 0730-2312

DOI - 10.1002/jcb.20537

Subject(s) - beamline , synchrotron radiation , microbeam , grazing incidence small angle scattering , nucleation , synchrotron , materials science , crystallography , scattering , diffraction , protein crystallization , optics , chemistry , physics , crystallization , beam (structure) , inelastic scattering , organic chemistry , x ray raman scattering

Ultrasmall P450scc cytochrome microcrystals are grown by classical hanging vapor diffusion and by its modification using homologous protein thin‐film template displaying a long‐range order. The nucleation and growth mechanisms of P450scc microcrystals are studied at the thin cytochrome film surface by a new microbeam grazing incidence small angle X‐ray scattering (µGISAXS) technique developed at the microfocus beamline of the European Synchrotron Radiation Facility (ESRF) in Grenoble, France. P450scc cytochrome crystals of about 5 µm are also investigated by synchrotron radiation diffraction in order to attempt a preliminary analysis of the atomic structure of this unique protein system yet unsolved. J. Cell. Biochem. 97: 544–552, 2006. © 2005 Wiley‐Liss, Inc.

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