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Determining the Molecular-packing Arrangements on Protein Crystal Faces by Atomic Force Microscopy by Huayu Li; Mary A. Perozzo; John H. Konnert; Arunan Nadarajah; Marc L. Pusey is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Determining the Molecular-packing Arrangements on Protein Crystal Faces by Atomic Force Microscopy about?

Previous atomic force microscopy (AFM) studies and periodic bond-chain (PBC) analyses of tetragonal lysozyme crystals have suggested that the (110) face consists of chains of molecules related to one another by 4 3 axes parallel to the crystal face. In this study, high-resolution AFM images of the (110) face were obtained and analyzed in order to verify this prediction. A computer program was employed which constructs the theoretical AFM image corresponding to a speci®c crystallographic molecular-packing arrangement and AFM tip shape. The packing arrangement and tip shape were varied in order to obtain the maximum possible correlation between experimental and theoretical images. The prediction from PBC analysis of an arrangement involving 4 3 helices was con®rmed in this manner, while the alternate arrangement, consisting of molecules related to one another by 2 1 axes, was not observed. However, the surface structure was found to differ signi®cantly even from this crystallographic arrangement. The molecules were found to pack slightly closer about what will become the 4 3 axes within the interior of the crystal, suggesting the occurrence of surface reconstruction or rearrangement

Who reads Determining the Molecular-packing Arrangements on Protein Crystal Faces by Atomic Force Microscopy?

Author

Huayu Li; Mary A. Perozzo; John H. Konnert; Arunan Nadarajah; Marc L. Pusey

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)