title: Crystallization and preliminary X-ray crystallographic study of the human MST2 SARAH domain.
abstract: The SARAH domain at the C-terminus of human MST2 (residues 436-484) was overproduced and purified using an Escherichia coli expression system. The purified domain was crystallized using the hanging-drop vapour-diffusion technique. Two crystal forms were obtained. The crystals belonged to space group P2, with unit-cell parameters a = 62.0, b = 119.2, c = 62.0 Å, α = 90.0, β = 90.5, γ = 90.0°, or to space group P6(1)22, with unit-cell parameters a = 54.5, b = 54.5, c = 303.1 Å. These crystals diffracted to 2.7 and 3.0 Å resolution, respectively.
authors.affiliation: College of Pharmacy, Chungbuk National University, Cheongju 361-763, Republic of Korea.
authors.forename: Jinsue
authors.initials: J
authors.lastname: Song
authors.forename: Hyerim
authors.initials: H
authors.lastname: Hong
authors.forename: Saehae
authors.initials: S
authors.lastname: Choi
authors.forename: Yong Hee
authors.initials: YH
authors.lastname: Lee
authors.forename: Eiki
authors.initials: E
authors.lastname: Yamashita
authors.forename: Suk Chul
authors.initials: SC
authors.lastname: Bae
authors.forename: Il Yeong
authors.initials: IY
authors.lastname: Park
authors.forename: Soo Jae
authors.initials: SJ
authors.lastname: Lee
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D000090742:Serine-Threonine Kinase 3; D000099317:Hippo Kinases
chemical_list: D017346:Protein Serine-Threonine Kinases; D000090742:Serine-Threonine Kinase 3; C097835:STK3 protein, human; D000099317:Hippo Kinases
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