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

Hae Shin Dong Hae Shin, Kwang Yeon Hwang, Kyu Kim Kyeong Kyu Kim, S. Kim, R. M. Sweet, Won Suh 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 (V(m)) of 2.36 Å3/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.

Original languageEnglish
Pages (from-to)80-83
Number of pages4
JournalProteins: Structure, Function and Genetics
Volume19
Issue number1
DOIs
Publication statusPublished - 1994 May 24
Externally publishedYes

Keywords

  • crystals
  • maize protein
  • X-ray diffraction

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

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