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. 2007 Jul 1;63(Pt 7):579-81.
doi: 10.1107/S1744309107026152. Epub 2007 Jun 11.

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

SeungBum Kim  1 , Sangbum Joo, Hyun C Yoon, Yeonwoo Ryu, Kyeong Kyu Kim, T Doohun Kim
Affiliations

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

SeungBum Kim et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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 A 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 A, beta = 97.1 degrees.

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Figures

Figure 1
Figure 1
A crystal of Est25 grown in a solution containing 2.4 M sodium malonate. Crystal dimensions were 0.4 × 0.3 × 0.1 mm.
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