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Structure and growth of ultrasmall protein microcrystals by synchrotron radiation: II. µGISAX and microscopy of lysozyme

✍ Scribed by Eugenia Pechkova; Claudio Nicolini

Publisher: John Wiley and Sons
Year: 2006
Tongue: English
Weight: 229 KB
Volume: 97
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.20538

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✦ Synopsis

Abstract

The early steps of growth and nucleation of the lysozyme microcrystals by classical and nanotemplate‐based hanging vapor diffusion methods are studied using µGISAXS at the European Synchrotron Radiation Facility (ESRF) in Grenoble, France. Out‐of‐plane cuts in the Yoneda regions of the 2D scattering profiles point to the detection of ultrasmall lysozyme crystals by µGISAXS quite before than by light microscopy. Furthermore lysozyme crystal formation occurs quite earlier with the nanotemplate than with the classical method. Our data are compatible with two distinct modes of crystal nucleation and growth for P450sc and lysozyme. J. Cell. Biochem. © 2005 Wiley‐Liss, Inc.

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## Abstract 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