# cryoEM Administrative Supplement for Equipment

> **NIH NIH R35** · FLORIDA STATE UNIVERSITY · 2021 · $249,600

## Abstract

ABSTRACT
Funds are requested for the purchase of a revolutionary new camera, the Apollo, from Direct
Electron Ltd. that would enable the collection of large amounts of image data, currently obtained
in the form of “movies”. The ability to collect large amounts of data would broaden the types of
questions addressable in the PI's R35 grant currently focused on obtaining atomic resolution
images of thick filaments from striated muscle. Generally, thick filaments from all striated
muscles have four structurally distinct regions: (1) a 160 nm long bare zone in the center where
myosin tails are packed antiparallel to each other, (2) an A-band follows where myosin
molecules are arranged in a helical or quasi helical structure with the myosin tails packed in a
parallel arrangement, (3) a tapered end where the connecting filament, e.g. titin, connects the
thick filament to the Z-disk, and (4) features along the thick filament A-band from invertebrates
in particular, but also from vertebrates, that fail to follow the myosin molecule arrangement. The
helical arrangement of myosin in the A-band of invertebrate thick filaments facilitates an atomic
structure of the myosin tail and head arrangement by using all of the myosin axial repeats from
the end of the bare zone to the beginning of the tapered ends. However, the bare zone, the
transition from bare zone to helical arrangement, the tapered ends as well as additional features
that do not follow the myosin helical symmetry perform important roles in the assembly of thick
filaments. Features, such as the paramyosin of invertebrate thick filaments fail to follow the
myosin helical symmetry in the A-band and are poorly represented in cryoEM reconstructions.
Paramyosin in concert with other non-myosin proteins may function to determine the thick
filament length in invertebrates. Titin, myosin binding protein C and other non-myosin proteins
of vertebrate thick filaments also do not follow a regular pattern along the entire A-band.
Acquisition of a much faster camera capable of recording a 60-frame movie in a single second,
will provide the tool needed to obtain high resolution 3-D images of these features that are not
well represented if at all in structures solved by enforcing helical symmetry.

## Key facts

- **NIH application ID:** 10389992
- **Project number:** 3R35GM139616-01S1
- **Recipient organization:** FLORIDA STATE UNIVERSITY
- **Principal Investigator:** KENNETH ALLEN TAYLOR
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2021
- **Award amount:** $249,600
- **Award type:** 3
- **Project period:** 2021-01-01 → 2025-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10389992

## Citation

> US National Institutes of Health, RePORTER application 10389992, cryoEM Administrative Supplement for Equipment (3R35GM139616-01S1). Retrieved via AI Analytics 2026-05-28 from https://api.ai-analytics.org/grant/nih/10389992. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*