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Making the most of two crystals: Structural analysis of a conserved hypothetical protein using native gel screening and SAD phasing

Lookup NU author(s): Dr Mark Banfield


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The protein PAE2307 is a member of a protein family of unknown function which is conserved among a number of bacterial and archaeal species. The protein was overexpressed in Escherichia coli, purified and crystallized in two crystal forms. The prevalent form was twinned, but the other diffracted to 1.45 Å resolution. The non-twinned crystals proved difficult to reproduce, so screening of potential heavy-atom derivatives by native polyacrylamide gel electrophoresis was used to establish suitable derivatization conditions. This process enabled the production of a K2Pt(NO2)4 derivative that was used to collect a single-wavelength anomalous diffraction (SAD) data set from the only available crystal. Phase information of high quality was obtained, enabling the calculation of an interpretable electron-density map.

Publication metadata

Author(s): Banfield MJ; Lott JS; Sigrell J; Baker EN

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica D: Biological Crystallography

Year: 2003

Volume: 59

Issue: 12

Pages: 2242-2246

ISSN (print): 0907-4449

ISSN (electronic):

Publisher: Wiley-Blackwell Publishing, Inc.


DOI: 10.1107/S0907444903020584

PubMed id: 14646083


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