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Title: So how do you know you have a macromolecular complex?

Abstract

Structures of protein complexes offer some of the most interesting insights into biological processes. In this article, the methods required to show that the complex observed is the physiological one are investigated. Protein in crystal form is at an extremely high concentration and yet retains the complex secondary structure that defines an active protein. The protein crystal itself is made up of a repeating lattice of protein–protein and protein–solvent interactions. The problem that confronts any crystallographer is to identify those interactions that represent physiological interactions and those that do not. This review explores the tools that are available to provide such information using the original crystal liquor as a sample. The review is aimed at postgraduate and postdoctoral researchers who may well be coming up against this problem for the first time. Techniques are discussed that will provide information on the stoichiometry of complexes as well as low-resolution information on complex structure. Together, these data will help to identify the physiological complex.

Authors:
 [1]
  1. Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT (United Kingdom)
Publication Date:
OSTI Identifier:
22347985
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2483502; PUBLISHER-ID: ba5100; PMID: 17164522; OAI: oai:pubmedcentral.nih.gov:2483502; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; INTERACTIONS; PROTEINS; RESOLUTION; REVIEWS; SOLVENTS; STOICHIOMETRY

Citation Formats

Dafforn, Timothy R., E-mail: t.r.dafforn@bham.ac.uk. So how do you know you have a macromolecular complex?. Denmark: N. p., 2007. Web. doi:10.1107/S0907444906047044.
Dafforn, Timothy R., E-mail: t.r.dafforn@bham.ac.uk. So how do you know you have a macromolecular complex?. Denmark. doi:10.1107/S0907444906047044.
Dafforn, Timothy R., E-mail: t.r.dafforn@bham.ac.uk. Mon . "So how do you know you have a macromolecular complex?". Denmark. doi:10.1107/S0907444906047044.
@article{osti_22347985,
title = {So how do you know you have a macromolecular complex?},
author = {Dafforn, Timothy R., E-mail: t.r.dafforn@bham.ac.uk},
abstractNote = {Structures of protein complexes offer some of the most interesting insights into biological processes. In this article, the methods required to show that the complex observed is the physiological one are investigated. Protein in crystal form is at an extremely high concentration and yet retains the complex secondary structure that defines an active protein. The protein crystal itself is made up of a repeating lattice of protein–protein and protein–solvent interactions. The problem that confronts any crystallographer is to identify those interactions that represent physiological interactions and those that do not. This review explores the tools that are available to provide such information using the original crystal liquor as a sample. The review is aimed at postgraduate and postdoctoral researchers who may well be coming up against this problem for the first time. Techniques are discussed that will provide information on the stoichiometry of complexes as well as low-resolution information on complex structure. Together, these data will help to identify the physiological complex.},
doi = {10.1107/S0907444906047044},
journal = {Acta Crystallographica. Section D: Biological Crystallography},
number = Pt 1,
volume = 63,
place = {Denmark},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}
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