# X-ray instrumentation upgrade for single crystal diffraction and solution small angle scattering

> **NIH NIH S10** · PENNSYLVANIA STATE UNIVERSITY, THE · 2020 · $600,000

## Abstract

Project Summary/Abstract
The X-ray crystallography facility at Pennsylvania State University desperately needs to upgrade the aged
Rigaku macromolecular crystallography instrument and the outdated Bruker small molecule X-ray diffractometer
with a reconfiguration of the two available ports on the Rigaku MicroMax007 X-ray generator. The improvements
we wish to have on the right port are ‘Varimax-VHFarc)sec’ optics with higher flux suitable for small sized crystals
of around 40m, a typical size in our crystallization trials; a universal four-circle kappa goniometer for efficient
data collection; and a shutter-less, large area, highly sensitive HyPix-Arc 150° detector to detect weak diffraction
from macromolecular crystals. We also wish to upgrade to an oxford cryo-stream for cooling the crystals during
data collection. For the left port we wish to configure it for small angle X-ray scattering (SAXS) with the BioSAXS-
2000 2D-Kratky system. This upgrade will enable both small and macromolecular X-ray crystallography on the
right port and add a new capability, solution SAXS on the left port. SAXS technique has the advantage of
determining a low-resolution structure with a fast turnaround time and not having to grow crystals. We have
identified the Rigaku components as the sole commercial product which meets our requirements, is state-of-the-
art and cost-effective. Having a higher X-ray flux and improved sensitivity is paramount for the success
and throughput of all the cutting-edge X-ray crystallography projects described in this proposal. The
controlling and analyzing software for both crystallography and SAXS provided by Rigaku is user friendly and
loaded with features for data processing and analysis. Upgrading the X-ray equipment is a desperate need to
the success of the twenty active NIH structural biology projects and two pending NIH grants participating in this
shared instrumentation proposal. This will enhance all the forefront research projects listed in the summary tables
(a) small molecule drug development research in Sharma and Giri labs (b) structure-function of proteins and
their complexes with nucleic acids in Murakami, Tan and Krasilnikov labs (c) enable a unique anaerobic SAXS
tool for the metallobiochemistry group including Booker, Boal and Bollinger labs working with oxygen sensitive
proteins and (d) facilitate rapid access to in-house SAXS equipment for the RNA samples that are prone to
misfolding/aggregation being studied in the Bevilacqua, Showalter, Krasilnikov labs. With the upgraded single
crystal and SAXS ports we would be investing in true synergy where-in the whole becomes greater
than the sum of the parts. Experimental results from crystallography would guide the interpretation of SAXS and
low-resolution solvent envelope models as obtained from SAXS of protein-protein or protein - nucleic acid or
nucleic acid multimers could help in the crystallographic study of these complexes at higher resolution.

## Key facts

- **NIH application ID:** 9940147
- **Project number:** 1S10OD028589-01
- **Recipient organization:** PENNSYLVANIA STATE UNIVERSITY, THE
- **Principal Investigator:** Neela H. Yennawar
- **Activity code:** S10 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $600,000
- **Award type:** 1
- **Project period:** 2020-07-10 → 2021-07-09

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9940147

## Citation

> US National Institutes of Health, RePORTER application 9940147, X-ray instrumentation upgrade for single crystal diffraction and solution small angle scattering (1S10OD028589-01). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/9940147. Licensed CC0.

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