Crystallization and preliminary crystallographic studies of an antimicrobial protein from pharbitis nil

S. C. Ha; K. Min; J. C. Koo; Y. Kim; D. J. Yun; M. J. Cho; K. K. Kim

doi:10.1107/S090744490001516X

Crystallization and preliminary crystallographic studies of an antimicrobial protein from pharbitis nil

S. C. Ha
, K. Min
, J. C. Koo
, Y. Kim
, D. J. Yun
, M. J. Cho
, K. K. Kim^*

^*Corresponding author for this work

Biology Education

Gyeongsang National University

Research output: Contribution to journal › Journal article › peer-review

4 Scopus citations

Abstract

An antimicrobial protein from seeds of Pharbitis nil (Pn-AMP) which shows an antifungal activity towards several agriculturally important plant pathogens has been crystallized in the presence of equimolar N-acetylglucosamine with sodium citrate as precipitant. The crystal belongs to the hexagonal space group P6₁22 (or P6₅22), with unit-cell parameters a = b = 29.33 (5), c = 133.44 (12) Å. Native data were collected using a crystal at 100 K to a resolution of 1.78 Å.

Original language	English
Pages (from-to)	263-265
Number of pages	3
Journal	Acta Crystallographica - Section D Biological Crystallography
Volume	57
Issue number	2
DOIs	https://doi.org/10.1107/S090744490001516X
State	Published - 2001

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title = "Crystallization and preliminary crystallographic studies of an antimicrobial protein from pharbitis nil",

abstract = "An antimicrobial protein from seeds of Pharbitis nil (Pn-AMP) which shows an antifungal activity towards several agriculturally important plant pathogens has been crystallized in the presence of equimolar N-acetylglucosamine with sodium citrate as precipitant. The crystal belongs to the hexagonal space group P6122 (or P6522), with unit-cell parameters a = b = 29.33 (5), c = 133.44 (12) {\AA}. Native data were collected using a crystal at 100 K to a resolution of 1.78 {\AA}.",

author = "Ha, \{S. C.\} and K. Min and Koo, \{J. C.\} and Y. Kim and Yun, \{D. J.\} and Cho, \{M. J.\} and Kim, \{K. K.\}",

year = "2001",

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language = "English",

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pages = "263--265",

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

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T1 - Crystallization and preliminary crystallographic studies of an antimicrobial protein from pharbitis nil

AU - Ha, S. C.

AU - Min, K.

AU - Koo, J. C.

AU - Kim, Y.

AU - Yun, D. J.

AU - Cho, M. J.

AU - Kim, K. K.

PY - 2001

Y1 - 2001

N2 - An antimicrobial protein from seeds of Pharbitis nil (Pn-AMP) which shows an antifungal activity towards several agriculturally important plant pathogens has been crystallized in the presence of equimolar N-acetylglucosamine with sodium citrate as precipitant. The crystal belongs to the hexagonal space group P6122 (or P6522), with unit-cell parameters a = b = 29.33 (5), c = 133.44 (12) Å. Native data were collected using a crystal at 100 K to a resolution of 1.78 Å.

AB - An antimicrobial protein from seeds of Pharbitis nil (Pn-AMP) which shows an antifungal activity towards several agriculturally important plant pathogens has been crystallized in the presence of equimolar N-acetylglucosamine with sodium citrate as precipitant. The crystal belongs to the hexagonal space group P6122 (or P6522), with unit-cell parameters a = b = 29.33 (5), c = 133.44 (12) Å. Native data were collected using a crystal at 100 K to a resolution of 1.78 Å.

UR - https://www.scopus.com/pages/publications/0035125718

U2 - 10.1107/S090744490001516X

DO - 10.1107/S090744490001516X

M3 - Journal article

C2 - 11173474

AN - SCOPUS:0035125718

SN - 0907-4449

VL - 57

SP - 263

EP - 265

JO - Acta Crystallographica - Section D Biological Crystallography

JF - Acta Crystallographica - Section D Biological Crystallography

IS - 2

ER -

Crystallization and preliminary crystallographic studies of an antimicrobial protein from pharbitis nil

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