Title

Optimizing Direct Cryo-Mounting for Native SAD Structure Determination

Abstract

Structure determination of a protein via X-ray crystallography using Single-Wavelength Anomalous Diffraction has become relatively common. Cryo-cooled protein crystals are, however, known to be heterogeneous in cell dimensions and crystal order, which might be expected to impact SAD structure determination. To optimize structure determination, we investigated two different approaches of direct transfer of the protein crystal from the growth tray-the conventional approach, which rapidly transfers the protein crystal through the ambient air, and a vial-mounting technique designed to preserve the relative humidity local to the crystal until the moment of cooling. Results suggest that the vial-mounting technique can improve SAD efficiency as much as 2x over the conventional approach.

Faculty Sponsor

Douglas Juers

Tracks

poster

Terms of Use

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Location

Cordiner Hall

Presentation Type

Poster

Research Funding Source or OCS Program

Kaitlin Harrison: National Institutes of Health, Whitman BBMB Department, Whitman Physics Department

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Optimizing Direct Cryo-Mounting for Native SAD Structure Determination

Cordiner Hall

Structure determination of a protein via X-ray crystallography using Single-Wavelength Anomalous Diffraction has become relatively common. Cryo-cooled protein crystals are, however, known to be heterogeneous in cell dimensions and crystal order, which might be expected to impact SAD structure determination. To optimize structure determination, we investigated two different approaches of direct transfer of the protein crystal from the growth tray-the conventional approach, which rapidly transfers the protein crystal through the ambient air, and a vial-mounting technique designed to preserve the relative humidity local to the crystal until the moment of cooling. Results suggest that the vial-mounting technique can improve SAD efficiency as much as 2x over the conventional approach.

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