Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings

Dong Hae Shin; Kwang Yeon Hwang; Kyeong Kyu Kim; Sangsoo Kim; Robert M. Sweet; Se Won Suh

doi:10.1002/prot.340190111

Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings

Dong Hae Shin, Kwang Yeon Hwang, Kyeong Kyu Kim, Sangsoo Kim, Robert M. Sweet, Se Won Suh

Department of Pharmaceutical Sciences

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

4 Scopus citations

Abstract

Phospholipid transfer protein from maize seedlings has been crystallized using trisodium citrate as precipitant. The crystal belongs to the orthorhombic space group P2₁2₁2₁ with unit cell dimensions of a = 24.46 Å, b = 49.97 Å, and c = 69.99 Å. The presence of one molecule in the asymmetric unit gives a crystal volume per protein mass (V_m) of 2.36 Å ³/Da and a solvent content of 48% by volume. The X‐ray diffraction pattern extends at least to 1.6 Å Bragg spacing when exposed to both CuK_α and synchrotron X‐rays. A set of X‐ray data to approximately 1.9 Å Bragg spacing has been collected from a native crystal. © 1994 Wiley‐Liss, Inc.

Original language	English
Pages (from-to)	80-83
Number of pages	4
Journal	Proteins: Structure, Function and Bioinformatics
Volume	19
Issue number	1
DOIs	https://doi.org/10.1002/prot.340190111
State	Published - May 1994

Keywords

X‐ray diffraction
crystals
maize protein

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10.1002/prot.340190111

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title = "Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings",

abstract = "Phospholipid transfer protein from maize seedlings has been crystallized using trisodium citrate as precipitant. The crystal belongs to the orthorhombic space group P212121 with unit cell dimensions of a = 24.46 {\AA}, b = 49.97 {\AA}, and c = 69.99 {\AA}. The presence of one molecule in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.36 {\AA} 3/Da and a solvent content of 48% by volume. The X‐ray diffraction pattern extends at least to 1.6 {\AA} Bragg spacing when exposed to both CuKα and synchrotron X‐rays. A set of X‐ray data to approximately 1.9 {\AA} Bragg spacing has been collected from a native crystal. {\textcopyright} 1994 Wiley‐Liss, Inc.",

keywords = "X‐ray diffraction, crystals, maize protein",

author = "Shin, {Dong Hae} and Hwang, {Kwang Yeon} and Kim, {Kyeong Kyu} and Sangsoo Kim and Sweet, {Robert M.} and Suh, {Se Won}",

year = "1994",

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T1 - Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings

AU - Shin, Dong Hae

AU - Hwang, Kwang Yeon

AU - Kim, Kyeong Kyu

AU - Kim, Sangsoo

AU - Sweet, Robert M.

AU - Suh, Se Won

PY - 1994/5

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AB - Phospholipid transfer protein from maize seedlings has been crystallized using trisodium citrate as precipitant. The crystal belongs to the orthorhombic space group P212121 with unit cell dimensions of a = 24.46 Å, b = 49.97 Å, and c = 69.99 Å. The presence of one molecule in the asymmetric unit gives a crystal volume per protein mass (Vm) of 2.36 Å 3/Da and a solvent content of 48% by volume. The X‐ray diffraction pattern extends at least to 1.6 Å Bragg spacing when exposed to both CuKα and synchrotron X‐rays. A set of X‐ray data to approximately 1.9 Å Bragg spacing has been collected from a native crystal. © 1994 Wiley‐Liss, Inc.

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JO - Proteins: Structure, Function and Bioinformatics

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Crystallization and preliminary X‐ray crystallographic analysis of phospholipid transfer protein from maize seedlings

Abstract

Keywords

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