Crystallization of an endochitinase from Hordeum vulgare L. seeds

P. John Hart; Michael P. Ready; Jon D. Robertus

doi:10.1016/0022-2836(92)90942-D

Crystallization of an endochitinase from Hordeum vulgare L. seeds

P. John Hart, Michael P. Ready, Jon D. Robertus

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

2 Scopus citations

Abstract

Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for high-resolution X-ray analysis. Crystals were grown by vapor diffusion under several different conditions. The best crystals, obtained with ammonium sulfate as the precipitant, belong to the tetragonal space group P4₁2₁2₁ (P4₃2₁2). with cell dimensions a = b = 62.9 A ̊and c = 96.0 A ̊. The cell dimensions are consistent with one endochitinase molecule per asymmetric unit, and the crystals diffract to at least 2.0 Å resolution.

Original language	English (US)
Pages (from-to)	565-567
Number of pages	3
Journal	Journal of Molecular Biology
Volume	225
Issue number	2
DOIs	https://doi.org/10.1016/0022-2836(92)90942-D
State	Published - May 20 1992
Externally published	Yes

Keywords

X-ray analysis
barley
crystallization
endochitinase

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0022-2836(92)90942-D

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@article{8f86da2bf2824d59b31c4a34a4189c66,

title = "Crystallization of an endochitinase from Hordeum vulgare L. seeds",

abstract = "Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for high-resolution X-ray analysis. Crystals were grown by vapor diffusion under several different conditions. The best crystals, obtained with ammonium sulfate as the precipitant, belong to the tetragonal space group P412121 (P43212). with cell dimensions a = b = 62.9 A ̊and c = 96.0 A ̊. The cell dimensions are consistent with one endochitinase molecule per asymmetric unit, and the crystals diffract to at least 2.0 {\AA} resolution.",

keywords = "X-ray analysis, barley, crystallization, endochitinase",

author = "Hart, {P. John} and Ready, {Michael P.} and Robertus, {Jon D.}",

note = "Funding Information: FZ{\textquoteright}r are grateful to Rayuelle Smalley for her htllp in preparing the Figures. This work was supported by grant (:M1;130048 from the National Institutes of Health and by R grant from the Foundation for Kesearch",

year = "1992",

month = may,

day = "20",

doi = "10.1016/0022-2836(92)90942-D",

language = "English (US)",

volume = "225",

pages = "565--567",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

number = "2",

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TY - JOUR

T1 - Crystallization of an endochitinase from Hordeum vulgare L. seeds

AU - Hart, P. John

AU - Ready, Michael P.

AU - Robertus, Jon D.

N1 - Funding Information: FZ’r are grateful to Rayuelle Smalley for her htllp in preparing the Figures. This work was supported by grant (:M1;130048 from the National Institutes of Health and by R grant from the Foundation for Kesearch

PY - 1992/5/20

Y1 - 1992/5/20

N2 - Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for high-resolution X-ray analysis. Crystals were grown by vapor diffusion under several different conditions. The best crystals, obtained with ammonium sulfate as the precipitant, belong to the tetragonal space group P412121 (P43212). with cell dimensions a = b = 62.9 A ̊and c = 96.0 A ̊. The cell dimensions are consistent with one endochitinase molecule per asymmetric unit, and the crystals diffract to at least 2.0 Å resolution.

AB - Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for high-resolution X-ray analysis. Crystals were grown by vapor diffusion under several different conditions. The best crystals, obtained with ammonium sulfate as the precipitant, belong to the tetragonal space group P412121 (P43212). with cell dimensions a = b = 62.9 A ̊and c = 96.0 A ̊. The cell dimensions are consistent with one endochitinase molecule per asymmetric unit, and the crystals diffract to at least 2.0 Å resolution.

KW - X-ray analysis

KW - barley

KW - crystallization

KW - endochitinase

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U2 - 10.1016/0022-2836(92)90942-D

DO - 10.1016/0022-2836(92)90942-D

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SN - 0022-2836

VL - 225

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EP - 567

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

Crystallization of an endochitinase from Hordeum vulgare L. seeds

Abstract

Keywords

ASJC Scopus subject areas

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