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

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 (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.

Original languageEnglish
Pages (from-to)80-83
Number of pages4
JournalProteins: Structure, Function, and Bioinformatics
Volume19
Issue number1
DOIs
Publication statusPublished - 1994 May
Externally publishedYes

Keywords

  • X‐ray diffraction
  • crystals
  • maize protein

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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