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Expression, refolding and crystallization of Aquifex aeolicus elongation factor P.

Kristensen, Ole and Laurberg, Martin LU (2002) In Acta Crystallographica. Section D: Biological Crystallography D58(Pt 6 Nr 2). p.1039-1041
Abstract
Elongation factor P is a universally conserved protein stimulating peptidyltransferase activity during protein synthesis. The factor is sensitive to classical inhibitors of the ribosomal peptidyltransferase activity and is possibly involved in alignment of the substrate tRNAs in the catalytic centre of 70S ribosomes. Elongation factor P from the thermophilic Aquifex aeolicus was overexpressed as a soluble protein in Escherichia coli and crystallized. A fast generally applicable refolding protocol was developed to improve crystal quality and circumvent strong binding of oligonucleotides to the protein. Diffraction data collected to 2.7 A resolution present twinning.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section D: Biological Crystallography
volume
D58
issue
Pt 6 Nr 2
pages
1039 - 1041
publisher
International Union of Crystallography
external identifiers
  • pmid:12037310
  • wos:000176271200018
  • scopus:0036075414
ISSN
1399-0047
DOI
10.1107/S0907444902005267
language
English
LU publication?
yes
id
071c369b-557d-4f8c-9a0b-90910b26e1cf (old id 108581)
date added to LUP
2007-07-09 15:41:02
date last changed
2017-01-01 07:17:31
@article{071c369b-557d-4f8c-9a0b-90910b26e1cf,
  abstract     = {Elongation factor P is a universally conserved protein stimulating peptidyltransferase activity during protein synthesis. The factor is sensitive to classical inhibitors of the ribosomal peptidyltransferase activity and is possibly involved in alignment of the substrate tRNAs in the catalytic centre of 70S ribosomes. Elongation factor P from the thermophilic Aquifex aeolicus was overexpressed as a soluble protein in Escherichia coli and crystallized. A fast generally applicable refolding protocol was developed to improve crystal quality and circumvent strong binding of oligonucleotides to the protein. Diffraction data collected to 2.7 A resolution present twinning.},
  author       = {Kristensen, Ole and Laurberg, Martin},
  issn         = {1399-0047},
  language     = {eng},
  number       = {Pt 6 Nr 2},
  pages        = {1039--1041},
  publisher    = {International Union of Crystallography},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {Expression, refolding and crystallization of Aquifex aeolicus elongation factor P.},
  url          = {http://dx.doi.org/10.1107/S0907444902005267},
  volume       = {D58},
  year         = {2002},
}