Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

Susanne C. Feil; Jamie Rossjohn; Kyle Rohde; Rodney K. Tweten; Michael W. Parker

doi:10.1016/S0014-5793(96)01200-8

Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

Susanne C. Feil, Jamie Rossjohn, Kyle Rohde, Rodney K. Tweten, Michael W. Parker

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

17 Citations (Scopus)

Abstract

We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin 0, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C222₁ with cell dimensions of a = 47.8 Å, b = 182.0 Å and c 175.5 Å and the crystals diffract to beyond 2.5 Å resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P222₁ with unit cell dimensions a = 47.1 Å, b = 166.1 Å and c = 214.0 Å and with diffraction observed to 2.4 Å resolution.

Original language	English
Pages (from-to)	290-292
Number of pages	3
Journal	FEBS Letters
Volume	397
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(96)01200-8
Publication status	Published - 18 Nov 1996
Externally published	Yes

Keywords

Crystallization
Perfringolysin 0
Pore-forming toxin
Thiol-activated cytolysin
X-ray diffraction

Access to Document

10.1016/S0014-5793(96)01200-8

Cite this

@article{567b1c3cfed544388e32709ffd514c99,

title = "Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin",

abstract = "We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin 0, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C2221 with cell dimensions of a = 47.8 {\AA}, b = 182.0 {\AA} and c 175.5 {\AA} and the crystals diffract to beyond 2.5 {\AA} resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P2221 with unit cell dimensions a = 47.1 {\AA}, b = 166.1 {\AA} and c = 214.0 {\AA} and with diffraction observed to 2.4 {\AA} resolution.",

keywords = "Crystallization, Perfringolysin 0, Pore-forming toxin, Thiol-activated cytolysin, X-ray diffraction",

author = "Feil, {Susanne C.} and Jamie Rossjohn and Kyle Rohde and Tweten, {Rodney K.} and Parker, {Michael W.}",

year = "1996",

month = nov,

day = "18",

doi = "10.1016/S0014-5793(96)01200-8",

language = "English",

volume = "397",

pages = "290--292",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons",

number = "2-3",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

AU - Feil, Susanne C.

AU - Rossjohn, Jamie

AU - Rohde, Kyle

AU - Tweten, Rodney K.

AU - Parker, Michael W.

PY - 1996/11/18

Y1 - 1996/11/18

N2 - We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin 0, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C2221 with cell dimensions of a = 47.8 Å, b = 182.0 Å and c 175.5 Å and the crystals diffract to beyond 2.5 Å resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P2221 with unit cell dimensions a = 47.1 Å, b = 166.1 Å and c = 214.0 Å and with diffraction observed to 2.4 Å resolution.

AB - We present the first reported crystallization of a member of the thiol-activated family of protein toxins. Perfringolysin 0, a virulence factor of Clostridium perfringens, has been crystallized in two different forms by the hanging drop vapor diffusion method. In one form the toxin crystallizes with PEG 20000 in the orthorhombic space group C2221 with cell dimensions of a = 47.8 Å, b = 182.0 Å and c 175.5 Å and the crystals diffract to beyond 2.5 Å resolution. In the second form the toxin crystallizes in a large variety of organic solvents including malt whisky. This crystal form belongs to the orthorhombic space group P2221 with unit cell dimensions a = 47.1 Å, b = 166.1 Å and c = 214.0 Å and with diffraction observed to 2.4 Å resolution.

KW - Crystallization

KW - Perfringolysin 0

KW - Pore-forming toxin

KW - Thiol-activated cytolysin

KW - X-ray diffraction

UR - http://www.scopus.com/inward/record.url?scp=0030592696&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(96)01200-8

DO - 10.1016/S0014-5793(96)01200-8

M3 - Article

C2 - 8955365

AN - SCOPUS:0030592696

SN - 0014-5793

VL - 397

SP - 290

EP - 292

JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

Crystallization and preliminary X-ray analysis of a thiol-activated cytolysin

Abstract

Keywords

Access to Document

Other files and links

Cite this