Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

Heli Nummelin; Yasmin El Tahir; Pauli Ollikka; Mikael Skurnik; Adrian Goldman

doi:10.1107/S0907444902005231

Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

Heli Nummelin, Yasmin El Tahir, Pauli Ollikka, Mikael Skurnik, Adrian Goldman^*

^*Corresponding author for this work

Animal and Veterinary Sciences

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Å, and diffract to 1.55 Å resolution on a synchrotron-radiation source.

Original language	English
Pages (from-to)	1042-1044
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	6 II
DOIs	https://doi.org/10.1107/S0907444902005231
Publication status	Published - 2002

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Biochemistry
Biophysics
Clinical Biochemistry
Structural Biology
Condensed Matter Physics

Access to Document

10.1107/S0907444902005231

Fingerprint Dive into the research topics of 'Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA'. Together they form a unique fingerprint.

Cite this

@article{07a4c6f8a2b1484fba5589b63b49ea77,

title = "Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA",

abstract = "A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 {\AA}, and diffract to 1.55 {\AA} resolution on a synchrotron-radiation source.",

author = "Heli Nummelin and {El Tahir}, Yasmin and Pauli Ollikka and Mikael Skurnik and Adrian Goldman",

year = "2002",

doi = "10.1107/S0907444902005231",

language = "English",

volume = "58",

pages = "1042--1044",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "John Wiley and Sons Inc.",

number = "6 II",

}

TY - JOUR

T1 - Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

AU - Nummelin, Heli

AU - El Tahir, Yasmin

AU - Ollikka, Pauli

AU - Skurnik, Mikael

AU - Goldman, Adrian

PY - 2002

Y1 - 2002

N2 - A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Å, and diffract to 1.55 Å resolution on a synchrotron-radiation source.

AB - A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Å, and diffract to 1.55 Å resolution on a synchrotron-radiation source.

UR - http://www.scopus.com/inward/record.url?scp=0036618133&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036618133&partnerID=8YFLogxK

U2 - 10.1107/S0907444902005231

DO - 10.1107/S0907444902005231

M3 - Article

C2 - 12037311

AN - SCOPUS:0036618133

VL - 58

SP - 1042

EP - 1044

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

SN - 0907-4449

IS - 6 II

ER -

Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this