Purification, crystallization, and preliminary crystallographic Analysis of Est25:a ketoprofen-specific hormone-sensitive-lipase
- Authors
- 김승범; 주상범; 윤현철; 유연우; 김경규; 김두헌
- Issue Date
- Jul-2007
- Publisher
- International Union of Crystallography
- Keywords
- Est25; ketoprofen-specific hormone-sensitive lipase.
- Citation
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v.63, no.7, pp 579 - 581
- Pages
- 3
- Journal Title
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Volume
- 63
- Number
- 7
- Start Page
- 579
- End Page
- 581
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159242
- DOI
- 10.1107/S1744309107026152
- ISSN
- 1744-3091
- 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°. © International Union of Crystallography 2007.
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