Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds

Kwang Yeon Hwang; Kyeong Kyu Kim; Kyeongsik Min; Soo Hyun Eom; Yeon Gyu Yu; Sangsoo Kim; Robert M. Sweet; Se Won Suh

doi:10.1006/jmbi.1993.1027

Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds

Kwang Yeon Hwang, Kyeong Kyu Kim, Kyeongsik Min, Soo Hyun Eom, Yeon Gyu Yu, Sangsoo Kim, Robert M. Sweet, Se Won Suh

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

5 Citations (Scopus)

Abstract

Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 AÅ upon exposure to synchrotron X-rays. The crystals belong to the space group P4₁2₁2 (or P4₃2₁2) with unit cell dimensions of a = 38.02 AÅ and c = 98.98 AÅ. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (V_m) of 1.99 AÅ³/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 AÅ Bragg spacing from native crystals.

Original language	English
Pages (from-to)	255-257
Number of pages	3
Journal	Journal of Molecular Biology
Volume	229
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.1993.1027
Publication status	Published - 1993 Jan 5
Externally published	Yes

Keywords

Crystallization
Phospholipid transfer protein
Possible amylase/protease inhibitor
Preliminary X-ray analysis
Rice seeds

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1006/jmbi.1993.1027

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title = "Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds",

abstract = "Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 A{\AA} upon exposure to synchrotron X-rays. The crystals belong to the space group P41212 (or P43212) with unit cell dimensions of a = 38.02 A{\AA} and c = 98.98 A{\AA}. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 A{\AA}3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 A{\AA} Bragg spacing from native crystals.",

keywords = "Crystallization, Phospholipid transfer protein, Possible amylase/protease inhibitor, Preliminary X-ray analysis, Rice seeds",

author = "Hwang, {Kwang Yeon} and Kim, {Kyeong Kyu} and Kyeongsik Min and Eom, {Soo Hyun} and Yu, {Yeon Gyu} and Sangsoo Kim and Sweet, {Robert M.} and Suh, {Se Won}",

year = "1993",

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day = "5",

doi = "10.1006/jmbi.1993.1027",

language = "English",

volume = "229",

pages = "255--257",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds

AU - Hwang, Kwang Yeon

AU - Kim, Kyeong Kyu

AU - Min, Kyeongsik

AU - Eom, Soo Hyun

AU - Yu, Yeon Gyu

AU - Kim, Sangsoo

AU - Sweet, Robert M.

AU - Suh, Se Won

PY - 1993/1/5

Y1 - 1993/1/5

N2 - Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 AÅ upon exposure to synchrotron X-rays. The crystals belong to the space group P41212 (or P43212) with unit cell dimensions of a = 38.02 AÅ and c = 98.98 AÅ. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 AÅ3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 AÅ Bragg spacing from native crystals.

AB - Large crystals of probable amylase/protease inhibitor-B have been grown at room temperature from ammonium sulfate solution. The crystals grow within five days to dimensions of 0.6 mm x 0.6 mm x 0.6 mm. They diffract to at least 1.7 AÅ upon exposure to synchrotron X-rays. The crystals belong to the space group P41212 (or P43212) with unit cell dimensions of a = 38.02 AÅ and c = 98.98 AÅ. The presence of one molecule per asymmetric unit gives the unit cell volume per protein mass (Vm) of 1.99 AÅ3/Da and the solvent fraction of 38.2% by volume. X-ray data have been collected to 2.0 AÅ Bragg spacing from native crystals.

KW - Crystallization

KW - Phospholipid transfer protein

KW - Possible amylase/protease inhibitor

KW - Preliminary X-ray analysis

KW - Rice seeds

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DO - 10.1006/jmbi.1993.1027

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SN - 0022-2836

VL - 229

SP - 255

EP - 257

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -

Crystallization and preliminary X-ray crystallographic analysis of probable amylase/protease inhibitor-B from rice seeds

Abstract

Keywords

ASJC Scopus subject areas

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