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Macromolecular Crystallographyconventional and high-throughput methods$
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Mark R. Sanderson and Jane V. Skelly

Print publication date: 2007

Print ISBN-13: 9780198520979

Published to Oxford Scholarship Online: September 2007

DOI: 10.1093/acprof:oso/9780198520979.001.0001

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Classical cloning, expression, and purification

Classical cloning, expression, and purification

(p.1) CHAPTER 1 Classical cloning, expression, and purification
Macromolecular Crystallography

Jane Skelly

Maninder K. Sohi

Thil Batuwangala

Oxford University Press

The ideal protein-expression strategy for X-ray structural analysis should provide correctly folded, soluble, and active protein in sufficient quantities for successful crystallization. Subsequent isolation and purification must be designed to achieve a polished product as rapidly as possible, involving a minimum number of steps. The simplest and least expensive methods employ bacterial hosts such as Escherichia coli, Bacillus, and Staphylococcus but if the target protein is from an eukaryotic source requiring post-translational processing for full functionality, an eukaryotic vector-host system would be appropriate. This chapter discusses the processes of cloning and expression, and protein extraction and isolation.

Keywords:   X-ray structural analysis, crystallization, cloning, expression, protein extraction, protein isolation

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