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Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescens

  • Kyeong Kyu Kim
  • , Kwang Yeon Hwang
  • , Kang Duk Choi
  • , Joo Hyun Kang
  • , Ook Joon Yoo
  • , Se Won Suh*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 × 0.7 × 0.6 mm3 within a month. The crystals belong to the trigonal space group P31 (or P32), with unit cell dimensions of a= 147.12 Å and c= 131.08 Å. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 Å3/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 Å Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 Å Bragg spacing from native crystals. © 1993 Wiley‐Liss, Inc.

Original languageEnglish
Pages (from-to)213-215
Number of pages3
JournalProteins: Structure, Function, and Bioinformatics
Volume15
Issue number2
DOIs
Publication statusPublished - 1993 Feb
Externally publishedYes

Keywords

  • X‐ray diffraction
  • bacterial esterase
  • crystals

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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