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Structure and growth of ultrasmall protein microcrystals by synchrotron radiation: II. µGISAX and microscopy of lysozyme
Author(s) -
Pechkova Eugenia,
Nicolini Claudio
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.20538
Subject(s) - lysozyme , nucleation , synchrotron radiation , protein crystallization , crystallography , synchrotron , crystal growth , scattering , microscopy , materials science , crystal (programming language) , chemistry , chemical physics , optics , physics , crystallization , biochemistry , programming language , organic chemistry , computer science
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.