System and method for forming synthetic protein crystals to determine the conformational structure by crystallography
Abstract
A method is disclosed for forming synthetic crystals of proteins in a carrier fluid by use of the dipole moments of protein macromolecules that self-align in the Helmholtz layer adjacent to an electrode. The voltage gradients of such layers easily exceed 10{sup 6}V/m. The synthetic protein crystals are subjected to x-ray crystallography to determine the conformational structure of the protein involved. 2 figs.
- Inventors:
- Issue Date:
- Research Org.:
- Univ. of California (United States)
- OSTI Identifier:
- 434168
- Patent Number(s):
- 5597457
- Application Number:
- PAN: 8-630,711
- Assignee:
- Univ. of California, Oakland, CA (United States)
- DOE Contract Number:
- W-7405-ENG-48
- Resource Type:
- Patent
- Resource Relation:
- Other Information: PBD: 28 Jan 1997
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 55 BIOLOGY AND MEDICINE, BASIC STUDIES; PROTEIN STRUCTURE; CRYSTALLOGRAPHY; MOLECULAR STRUCTURE; PROTEINS; CRYSTAL STRUCTURE
Citation Formats
Craig, G D, Glass, R, and Rupp, B. System and method for forming synthetic protein crystals to determine the conformational structure by crystallography. United States: N. p., 1997.
Web.
Craig, G D, Glass, R, & Rupp, B. System and method for forming synthetic protein crystals to determine the conformational structure by crystallography. United States.
Craig, G D, Glass, R, and Rupp, B. Tue .
"System and method for forming synthetic protein crystals to determine the conformational structure by crystallography". United States.
@article{osti_434168,
title = {System and method for forming synthetic protein crystals to determine the conformational structure by crystallography},
author = {Craig, G D and Glass, R and Rupp, B},
abstractNote = {A method is disclosed for forming synthetic crystals of proteins in a carrier fluid by use of the dipole moments of protein macromolecules that self-align in the Helmholtz layer adjacent to an electrode. The voltage gradients of such layers easily exceed 10{sup 6}V/m. The synthetic protein crystals are subjected to x-ray crystallography to determine the conformational structure of the protein involved. 2 figs.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Jan 28 00:00:00 EST 1997},
month = {Tue Jan 28 00:00:00 EST 1997}
}
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