title: Expression, purification, crystallization and preliminary X-ray analysis of the human NORE1 SARAH domain.
abstract: NORE1 is an important tumour suppressor in human cancers that interacts with the pro-apoptotic protein kinase MST1/2 through SARAH domains. The SARAH domain (residues 366-413) of human NORE1 was expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystal diffracted to 2.7 Å resolution and belonged to space group P6(1)22, with unit-cell parameters a = b = 73.041, c = 66.092 Å, α = β = 90, γ = 120°.
authors: Division of Magnetic Resonance, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang, Chungbuk 363-883, Republic of Korea.
authors: Hye Jin
authors: HJ
authors: Kim
authors: Eunha
authors: E
authors: Hwang
authors: Young-Hyun
authors: YH
authors: Han
authors: Saehae
authors: S
authors: Choi
authors: Woo Cheol
authors: WC
authors: Lee
authors: Hye-Yeon
authors: HY
authors: Kim
authors: Young Ho
authors: YH
authors: Jeon
authors: Chaejoon
authors: C
authors: Cheong
authors: Hae-Kap
authors: HK
authors: Cheong
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D051017:Apoptosis Regulatory Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006801:Humans; D020559:Monomeric GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D051017:Apoptosis Regulatory Proteins; C454042:RASSF5 protein, human; D020559:Monomeric GTP-Binding Proteins