Purification, crystallization and preliminary crystallographic analysis of Est25: A ketoprofen-specific hormone-sensitive lipase

  • Seung Bum Kim
  • , Sangbum Joo
  • , Hyun C. Yoon
  • , Yeonwoo Ryu
  • , Kyeong Kyu Kim
  • , T. Doohun Kim

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Ketoprofen, a nonsteroidal anti-inflammatory drug, inhibits the synthesis of prostaglandin. A novel hydrolase (Est25) with high ketoprofen specificity has previously been identified using a metagenomic library from environmental samples. Recombinant Est25 protein with a histidine tag at the N-terminus was expressed in Escherichia coli and purified in a homogenous form. Est25 was crystallized from 2.4 M sodium malonate pH 7.0 and X-ray diffraction data were collected to 1.49 Å using synchrotron radiation. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 197.8, b = 95.2, c = 99.4 Å, β = 97.1°.

Original languageEnglish
Pages (from-to)579-581
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number7
DOIs
StatePublished - 15 Jun 2007

Keywords

  • Est25
  • Ketoprofen-specific hormone-sensitive lipase

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