The University of Southampton
University of Southampton Institutional Repository

Crystallization and preliminary X-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain

Crystallization and preliminary X-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain
Crystallization and preliminary X-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain

A recombinant form of the variable domain of the α chain of a murine T- cell receptor specific for the N-terminal nonapeptide of myelin basin protein in association with the major histocompatibility complex class II I-A(u) molecule has been crystallized in a form suitable for X-ray diffraction analysis. This protein was secreted into the periplasmic space of Escherichia coli cells and affinity-purified using a nickel chelate adsorbent. The crystals are orthorhombic, space group P21212, with unit cell dimensions a=97.7 Å, b=79.6 Å, c=30.4 Å and diffract to beyond 2.2 Å resolution. The ability to crystallize a T-cell receptor domain produced in bacteria strongly suggests that the periplasmic space can provide a suitable environment for the correct in vivo folding of this class of antigen recognition molecules.

Crystallization, T-cell receptor, Vα domain, α chain
0022-2836
339-341
Fields, Barry A.
737f0eac-df6f-4433-9977-6297daa487a7
Ysern, Xavier
b185288d-519f-41cf-b20f-f7f3c9d85d40
Poljak, Roberto J.
54d15fd7-cf40-42fd-96a2-c6f03159865b
Shao, Xuguang
02d0b239-e3a1-4d8c-a7cd-07670b56969d
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Mariuzza, Roy A.
e81103c5-af20-4034-8d29-0c24b2a98b40
Fields, Barry A.
737f0eac-df6f-4433-9977-6297daa487a7
Ysern, Xavier
b185288d-519f-41cf-b20f-f7f3c9d85d40
Poljak, Roberto J.
54d15fd7-cf40-42fd-96a2-c6f03159865b
Shao, Xuguang
02d0b239-e3a1-4d8c-a7cd-07670b56969d
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Mariuzza, Roy A.
e81103c5-af20-4034-8d29-0c24b2a98b40

Fields, Barry A., Ysern, Xavier, Poljak, Roberto J., Shao, Xuguang, Ward, E. Sally and Mariuzza, Roy A. (1994) Crystallization and preliminary X-ray diffraction study of a bacterially produced T-cell antigen receptor Vα domain. Journal of Molecular Biology, 239 (2), 339-341. (doi:10.1006/jmbi.1994.1373).

Record type: Article

Abstract

A recombinant form of the variable domain of the α chain of a murine T- cell receptor specific for the N-terminal nonapeptide of myelin basin protein in association with the major histocompatibility complex class II I-A(u) molecule has been crystallized in a form suitable for X-ray diffraction analysis. This protein was secreted into the periplasmic space of Escherichia coli cells and affinity-purified using a nickel chelate adsorbent. The crystals are orthorhombic, space group P21212, with unit cell dimensions a=97.7 Å, b=79.6 Å, c=30.4 Å and diffract to beyond 2.2 Å resolution. The ability to crystallize a T-cell receptor domain produced in bacteria strongly suggests that the periplasmic space can provide a suitable environment for the correct in vivo folding of this class of antigen recognition molecules.

Full text not available from this repository.

More information

Published date: 2 June 1994
Keywords: Crystallization, T-cell receptor, Vα domain, α chain

Identifiers

Local EPrints ID: 425267
URI: https://eprints.soton.ac.uk/id/eprint/425267
ISSN: 0022-2836
PURE UUID: acc51539-d36f-418c-b0fa-c677e74c67d2
ORCID for E. Sally Ward: ORCID iD orcid.org/0000-0003-3232-7238

Catalogue record

Date deposited: 12 Oct 2018 16:30
Last modified: 22 May 2019 00:21

Export record

Altmetrics

Contributors

Author: Barry A. Fields
Author: Xavier Ysern
Author: Roberto J. Poljak
Author: Xuguang Shao
Author: E. Sally Ward ORCID iD
Author: Roy A. Mariuzza

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of https://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×