Expression, refolding and crystallization of Aquifex aeolicus elongation factor P.
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/108581
- author
- Kristensen, Ole and Laurberg, Martin LU
- organization
- publishing date
- 2002
- 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
- John Wiley & Sons Inc.
- 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
- 2016-04-01 16:52:15
- date last changed
- 2022-02-28 00:16:26
@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 = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1107/S0907444902005267}}, volume = {{D58}}, year = {{2002}}, }