Expression, refolding and crystallization of Aquifex aeolicus elongation factor P

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Expression, refolding and crystallization of Aquifex aeolicus elongation factor P. / Kristensen, Ole; Laurberg, Martin.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 58, No. Pt 6 Pt 2, 2002, p. 1039-41.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kristensen, O & Laurberg, M 2002, 'Expression, refolding and crystallization of Aquifex aeolicus elongation factor P', Acta Crystallographica. Section D: Biological Crystallography, vol. 58, no. Pt 6 Pt 2, pp. 1039-41.

APA

Kristensen, O., & Laurberg, M. (2002). Expression, refolding and crystallization of Aquifex aeolicus elongation factor P. Acta Crystallographica. Section D: Biological Crystallography, 58(Pt 6 Pt 2), 1039-41.

Vancouver

Kristensen O, Laurberg M. Expression, refolding and crystallization of Aquifex aeolicus elongation factor P. Acta Crystallographica. Section D: Biological Crystallography. 2002;58(Pt 6 Pt 2):1039-41.

Author

Kristensen, Ole ; Laurberg, Martin. / Expression, refolding and crystallization of Aquifex aeolicus elongation factor P. In: Acta Crystallographica. Section D: Biological Crystallography. 2002 ; Vol. 58, No. Pt 6 Pt 2. pp. 1039-41.

Bibtex

@article{6fc8179128a94ea1971a056b5227d1a3,
title = "Expression, refolding and crystallization of Aquifex aeolicus elongation factor P",
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.",
keywords = "Bacterial Proteins, Crystallization, Crystallography, X-Ray, Gene Expression, Peptide Elongation Factors, Protein Conformation, Protein Folding",
author = "Ole Kristensen and Martin Laurberg",
year = "2002",
language = "English",
volume = "58",
pages = "1039--41",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 6 Pt 2",

}

RIS

TY - JOUR

T1 - Expression, refolding and crystallization of Aquifex aeolicus elongation factor P

AU - Kristensen, Ole

AU - Laurberg, Martin

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - Bacterial Proteins

KW - Crystallization

KW - Crystallography, X-Ray

KW - Gene Expression

KW - Peptide Elongation Factors

KW - Protein Conformation

KW - Protein Folding

M3 - Journal article

C2 - 12037310

VL - 58

SP - 1039

EP - 1041

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 6 Pt 2

ER -

ID: 40318775