# Administrative Supplement for Equipment: Amersham Typhoon 5 Gel and Blot Imager

> **NIH NIH R35** · TEXAS TECH UNIVERSITY · 2020 · $125,000

## Abstract

Abstract.
The research program of the Latham Laboratory centers on understanding the relationship between structure,
dynamics, and function. We are particularly interested in examining this relationship in large macromolecular
assemblies, which have for the most part been recalcitrant to detailed structural and dynamics studies. We
couple high-resolution methyl-based nuclear magnetic resonance (NMR) spectroscopy, which is capable of
probing macromolecules up to ~1 MDa in size, with other biophysical (e.g., lanthanide resonance energy
transfer – LRET) and biochemical techniques to better understand function. Currently, the focus of our program
is on two protein complexes that bind to nucleic acids: the universally conserved and essential DNA double
strand break repair complex Mre11-Rad50-Nbs1 (MRN) and the mRNA cleavage and poly-adenylation
assembly cleavage stimulation factor complex (CstF). In both cases, existing structural and biochemical
studies have suggested a role for protein motions in the function of the complex. However, many questions still
remain about the interplay of structure and dynamics and how these relate to and control MRN and CstF
activity. For the MRN complex, X-ray crystallography, cryo-electron microscopy, and small angle X-ray
scattering studies have shown large structural changes within the complex upon ATP binding and have also
hinted at local domain motions upon dsDNA binding; however, the timescale of these movements, other key
structural states, their importance in function, and local dynamics have not been described. Similarly for the
CstF complex, X-ray crystallography and NMR spectroscopy on isolated domains have given views of local
structure and dynamics and provided a clue for nascent mRNA recognition; yet, the architecture of the full
complex and complete structure of the RNA-bound state is missing. Additionally, disease associated mutations
have been noted for both the MRN and CstF complexes. Thus, a main goal of the parent grant is to describe
the structures and dynamics of these two nucleic acid binding complexes to better understand the how these
characteristics affect function.

## Key facts

- **NIH application ID:** 10135620
- **Project number:** 3R35GM128906-02S1
- **Recipient organization:** TEXAS TECH UNIVERSITY
- **Principal Investigator:** Michael Parker Latham
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $125,000
- **Award type:** 3
- **Project period:** 2018-09-01 → 2023-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10135620

## Citation

> US National Institutes of Health, RePORTER application 10135620, Administrative Supplement for Equipment: Amersham Typhoon 5 Gel and Blot Imager (3R35GM128906-02S1). Retrieved via AI Analytics 2026-05-25 from https://api.ai-analytics.org/grant/nih/10135620. Licensed CC0.

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