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 journalArticlepeer-review

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
StatePublished - May 1994
Externally publishedYes

Keywords

  • crystals
  • maize protein
  • X‐ray diffraction

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