skip to main content

Title: Selenium incorporation using recombinant techniques

An overview of techniques for recombinant incorporation of selenium and subsequent purification and crystallization of the resulting labelled protein. Using selenomethionine to phase macromolecular structures is common practice in structure determination, along with the use of selenocysteine. Selenium is consequently the most commonly used heavy atom for MAD. In addition to the well established recombinant techniques for the incorporation of selenium in prokaryal expression systems, there have been recent advances in selenium labelling in eukaryal expression, which will be discussed. Tips and things to consider for the purification and crystallization of seleno-labelled proteins are also included.
Authors:
 [1]
  1. Protein Structure and Function Laboratory, Cancer Research UK London Research Institute, Lincoln’s Inn Fields, London WC2A 3PX (United Kingdom)
Publication Date:
OSTI Identifier:
22347933
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 66; Journal Issue: Pt 4; Other Information: PMCID: PMC2852298; PMID: 20382987; PUBLISHER-ID: ba5133; OAI: oai:pubmedcentral.nih.gov:2852298; Copyright (c) Walden 2010; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ATOMS; CRYSTALLIZATION; CRYSTALS; PROTEINS; SELENIUM