New York Consortium on Membrane Protein Structure:


A fluorescence-detection size-exclusion chromatography-based thermostability assay for membrane protein precrystallization screening.

New York Consortium on Membrane Protein Structure

Optimization of membrane protein stability under different solution conditions is essential for obtaining crystals that diffract to high resolution. Here we present a rapid and efficient fluorescence-detection size-exclusion chromatography-based thermostability assay (FSEC-TS) where the target protein is fused to GFP.

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Enhancing anomalous diffraction signals for solving membrane protein structures and complexes

New York Consortium on Membrane Protein Structure

We are developing diffraction technologies for structural analysis of particularly challenging systems by using the strengthened anomalous signals realized from sensible multi-crystal averaging. Our analyses support the likely prospect of solving challenging structures by combining data from several to many crystals to enhance the signal-to-noise ratio from anomalous diffraction. Although we applied the method primarily to multiple selenomethionyl and native crystals for SAD phasing, the method in general should enhance measurement of weak anomalous signals from any type of anomalous scatterer.

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Lipidic cubic phase-dispensing robot

New York Consortium on Membrane Protein Structure

NYCOMPS has constructed an economical lipidic cubic phase (LCP)-dispensing robot.

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LocTree2 predicts localization for all domains of life

New York Consortium on Membrane Protein Structure

Subcellular localization is one aspect of protein function. Despite advances in high-throughput imaging, localization maps remain incomplete. LocTree2 uses a hierarchical system of support vector machines that imitate the cascading mechanism of cellular sorting.

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New York Consortium on Membrane Protein Sturcture

New York Consortium on Membrane Protein Structure

New York Consortium on Membrane Protein Structure (NYCOMPS)

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