Book Review of X-ray Crystallography of Biomacromolecules: A Practical Guide X-Ray Crystallography of Biomacromolecules: A Practical Guide.  By Albrecht Messerschmidt  (Max-Planck-Institute for Biochemistry, Martinsried, Germany).   Wiley-VCH Verlag GmbH & Co. KGaA:   Weinheim 2007 .  xiii + 304  pp. $175. ISBN: 978-3-527-31396-9 .

2008 ◽  
Vol 130 (31) ◽  
pp. 10447-10447
Author(s):  
Jon Robertus
Keyword(s):  
Max Planck ◽  
X Ray ◽  
X Ray Crystallography ◽  
Practical Guide

scholarly journals Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography

Methods ◽  
2009 ◽  
Vol 49 (2) ◽  
pp. 174-180 ◽  
Author(s):  
Leonardo G. Trabuco ◽  
Elizabeth Villa ◽  
Eduard Schreiner ◽  
Christopher B. Harrison ◽  
Klaus Schulten
Keyword(s):  
Electron Microscopy ◽  
Molecular Dynamics ◽  
X Ray ◽  
X Ray Crystallography ◽  
Practical Guide ◽  
Cryo Electron Microscopy

Difference Fourier Analysis of Glucose Embedded and Frozen Hydrated Purple Membrane

1982 ◽  
Vol 40 ◽  
pp. 74-75
Author(s):  
Jules S. Jaffe ◽  
Robert M. Glaeser
Keyword(s):  
Purple Membrane ◽  
Data Set ◽  
High Resolution Data ◽  
X Ray ◽  
X Ray Crystallography ◽  
Fourier Techniques ◽  
Versus Protein ◽  
The Difference ◽  
Difference Fourier ◽  
Ideal Method

Although difference Fourier techniques are standard in X-ray crystallography it has only been very recently that electron crystallographers have been able to take advantage of this method. We have combined a high resolution data set for frozen glucose embedded Purple Membrane (PM) with a data set collected from PM prepared in the frozen hydrated state in order to visualize any differences in structure due to the different methods of preparation. The increased contrast between protein-ice versus protein-glucose may prove to be an advantage of the frozen hydrated technique for visualizing those parts of bacteriorhodopsin that are embedded in glucose. In addition, surface groups of the protein may be disordered in glucose and ordered in the frozen state. The sensitivity of the difference Fourier technique to small changes in structure provides an ideal method for testing this hypothesis.

3-D reconstruction of molecular shape from microcrystal thin sections

1983 ◽  
Vol 41 ◽  
pp. 748-749
Author(s):  
S. Cusack ◽  
J.-C. Jésior
Keyword(s):  
Three Dimensional ◽  
Molecular Shape ◽  
Biological Molecules ◽  
Fourier Space ◽  
Single Particles ◽  
Thin Sections ◽  
Standard Methods ◽  
X Ray ◽  
X Ray Crystallography ◽  
Dimensional Reconstruction

Three-dimensional reconstruction techniques using electron microscopy have been principally developed for application to 2-D arrays (i.e. monolayers) of biological molecules and symmetrical single particles (e.g. helical viruses). However many biological molecules that crystallise form multilayered microcrystals which are unsuitable for study by either the standard methods of 3-D reconstruction or, because of their size, by X-ray crystallography. The grid sectioning technique enables a number of different projections of such microcrystals to be obtained in well defined directions (e.g. parallel to crystal axes) and poses the problem of how best these projections can be used to reconstruct the packing and shape of the molecules forming the microcrystal.Given sufficient projections there may be enough information to do a crystallographic reconstruction in Fourier space. We however have considered the situation where only a limited number of projections are available, as for example in the case of catalase platelets where three orthogonal and two diagonal projections have been obtained (Fig. 1).

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