Literature DB >> 16215973

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

Eugenia Pechkova1, Claudio Nicolini.   

Abstract

The early steps of growth and nucleation of the lysozyme microcrystals by classical and nanotemplate-based hanging vapor diffusion methods are studied using microGISAXS 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 microGISAXS 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. (c) 2005 Wiley-Liss, Inc.

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Year:  2006        PMID: 16215973     DOI: 10.1002/jcb.20538

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  3 in total

1.  In situ muGISAXS: I. Experimental setup for submicron study of protein nucleation and growth.

Authors:  Ronald Gebhardt; Eugenia Pechkova; Christian Riekel; Claudio Nicolini
Journal:  Biophys J       Date:  2010-08-09       Impact factor: 4.033

2.  In situ muGISAXS: II. Thaumatin crystal growth kinetic.

Authors:  Ronald Gebhardt; Eugenia Pechkova; Christian Riekel; Claudio Nicolini
Journal:  Biophys J       Date:  2010-08-09       Impact factor: 4.033

3.  Langmuir-Blodgett nanotemplates for protein crystallography.

Authors:  Eugenia Pechkova; Claudio Nicolini
Journal:  Nat Protoc       Date:  2017-11-30       Impact factor: 13.491

  3 in total

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