ABSTRACT
Recent atomic scale characterization of Langmuir-Blodgett (LB)-based protein crystals here reviewed, namely via laser-microdissection, Raman spectroscopy, in situ grazing-incidence small-angle X-ray scattering, atomic force microscopy, and synchrotron radiation diffraction down to the nanofocus scale, provides new and unexpected insights on the role of LB nano-template on protein crystal domain organization, nucleation, and growth. These insights are quite superior to the already Synchrotron Radiation and Structural Proteomics Edited by Eugenia Pechkova and Christian Riekel Copyright © 2012 Pan Stanford Publishing Pte. Ltd. www.panstanford.com
significant properties discovered five years ago which led to proteins being uniquely crystallizable only with LB nanotemplate (CK2α ki-nase and P450scc). They complement the recently discovered unique radiation resistance for crystals of six model proteins reported in this volume. The major challenges here successfully addressed with LB nanotemplate proved to be the lack of crystallization (for the first time with IF2α and β, ribosomal protein, phage GroEL), and the domains identification and characterization.
