Paper Report for: Kim_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_579
Reference
Title: Purification, crystallization and preliminary crystallographic analysis of Est25: a ketoprofen-specific hormone-sensitive lipase Kim S, Joo S, Yoon HC, Ryu Y, Kim KK, Kim TD Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 63:579, 2007 : PubMed
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.
Kim S, Joo S, Yoon HC, Ryu Y, Kim KK, Kim TD (2007) Purification, crystallization and preliminary crystallographic analysis of Est25: a ketoprofen-specific hormone-sensitive lipase Acta Crystallographica Sect F Struct Biol Cryst Commun63: 579-81
Kim S, Joo S, Yoon HC, Ryu Y, Kim KK, Kim TD (2007) Acta Crystallographica Sect F Struct Biol Cryst Commun63: 579-81