# Optimization of Membrane Protein Samples for Structural Analysis (502-547)

> **NIH NIH P41** · NEW YORK STRUCTURAL BIOLOGY CENTER · 2020 · $111,890

## Abstract

In this section, we will develop novel technologies and approaches to increase the success rate of integral
membrane protein structure determination by x-ray crystallography and cryo-electron microscopy (cryo-EM).
The focus will be on sample preparation. Three of the four methods described depend on sequence
optimization of the target membrane protein, either by (1) identifying and expanding upon regions of genomic
sequence space most likely to harbor proteins amenable to in-depth structural analysis; (2) by producing
libraries of random mutants of the target protein, and selecting those with increased probability of success in
structure determination; (3) by genetically engineering chimeras between integral membrane proteins and
soluble chaperones to promote either crystallization in lipidic cubic phase, or large molecular-weight
assemblies for cryo-EM structure determination. In (4), we describe high-throughput screening methods to identify
appropriate samples for high-resolution cryo-EM structure determination.

## Key facts

- **NIH application ID:** 9939553
- **Project number:** 5P41GM116799-05
- **Recipient organization:** NEW YORK STRUCTURAL BIOLOGY CENTER
- **Principal Investigator:** WAYNE A. HENDRICKSON
- **Activity code:** P41 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $111,890
- **Award type:** 5
- **Project period:** — → 2022-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9939553

## Citation

> US National Institutes of Health, RePORTER application 9939553, Optimization of Membrane Protein Samples for Structural Analysis (502-547) (5P41GM116799-05). Retrieved via AI Analytics 2026-06-03 from https://api.ai-analytics.org/grant/nih/9939553. Licensed CC0.

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