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Fusion Proteins as Alternate Crystallization Paths to Difficult Structure Problems

Year: 1994

Type: article

Abstract: The three-dimensional structure of a peptide fusion product with glutathione transferase from Schisro.wma japonicum (SjGST) has been solved by crystallographic methods to 2.5 Å resolution. Pcptidcs or proteins can he fused to SjGST and expressed in a plasmid for rapid synthesis in Escherichia coli. Fusion proteins created hy this commercial method can be purified rapidly by chromatography on immobilized glutathione. The potential utility of using SjGST fusion proteins as alternate paths to the crystallization and structure determination of proteins is demonstrated.

Source: Protein and Peptide Letters

DOI: 10.2174/0929866501666220425002811

Authors: Daniel C. Carter, Florian Riiker, Joseph X. Ho, Kap Lim, Kim Keeling, Gary Gilliland, Xinhua Ji

Institutions: Marshall Space Flight Center, National Aeronautics and Space Administration, BOKU University

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W293129461

FWCI: 2.013

Cites:

Cited by: 11

Related to: 10