Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds

Kyu Song Hyun Kyu Song; Yeon Hwang Kwang Yeon Hwang; Kyu Kim Kyeong Kyu Kim; Won Suh Se Won Suh

doi:10.1002/prot.340170113

Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds

Kyu Song Hyun Kyu Song, Yeon Hwang Kwang Yeon Hwang, Kyu Kim Kyeong Kyu Kim, Won Suh Se Won Suh

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

2 Citations (Scopus)

Abstract

Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P2₁, with unit cell parameters of a = 69.43 Å, b = 44.55 Å, c = 81.41 Å, and β = 111.95°. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (V(M)) of 2.25 Å³/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 Å with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 Å Bragg spacing from a native crystal.

Original language	English
Pages (from-to)	107-109
Number of pages	3
Journal	Proteins: Structure, Function and Genetics
Volume	17
Issue number	1
DOIs	https://doi.org/10.1002/prot.340170113
Publication status	Published - 1993
Externally published	Yes

Keywords

X-ray diffraction
antifungal protein
crystals
plant chitinase

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.340170113

Cite this

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title = "Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds",

abstract = "Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P21, with unit cell parameters of a = 69.43 {\AA}, b = 44.55 {\AA}, c = 81.41 {\AA}, and β = 111.95°. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (V(M)) of 2.25 {\AA}3/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 {\AA} with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 {\AA} Bragg spacing from a native crystal.",

keywords = "X-ray diffraction, antifungal protein, crystals, plant chitinase",

author = "{Hyun Kyu Song}, {Kyu Song} and {Kwang Yeon Hwang}, {Yeon Hwang} and {Kyeong Kyu Kim}, {Kyu Kim} and {Se Won Suh}, {Won Suh}",

year = "1993",

doi = "10.1002/prot.340170113",

language = "English",

volume = "17",

pages = "107--109",

journal = "Proteins: Structure, Function and Genetics",

issn = "0887-3585",

publisher = "John Wiley and Sons Inc.",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds

AU - Hyun Kyu Song, Kyu Song

AU - Kwang Yeon Hwang, Yeon Hwang

AU - Kyeong Kyu Kim, Kyu Kim

AU - Se Won Suh, Won Suh

PY - 1993

Y1 - 1993

N2 - Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P21, with unit cell parameters of a = 69.43 Å, b = 44.55 Å, c = 81.41 Å, and β = 111.95°. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (V(M)) of 2.25 Å3/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 Å with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 Å Bragg spacing from a native crystal.

AB - Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P21, with unit cell parameters of a = 69.43 Å, b = 44.55 Å, c = 81.41 Å, and β = 111.95°. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (V(M)) of 2.25 Å3/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 Å with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 Å Bragg spacing from a native crystal.

KW - X-ray diffraction

KW - antifungal protein

KW - crystals

KW - plant chitinase

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U2 - 10.1002/prot.340170113

DO - 10.1002/prot.340170113

M3 - Article

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SN - 0887-3585

VL - 17

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EP - 109

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

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Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds

Abstract

Keywords

ASJC Scopus subject areas

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