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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, ? = ? = 90, ? = 120°.

SUBMITTER: Kim HJ

PROVIDER: S-EPMC3388929 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray analysis of the human NORE1 SARAH domain.

Kim Hye Jin HJ Hwang Eunha E Han Young-Hyun YH Choi Saehae S Lee Woo Cheol WC Kim Hye-Yeon HY Jeon Young Ho YH Cheong Chaejoon C Cheong Hae-Kap HK

Acta crystallographica. Section F, Structural biology and crystallization communications 20120628 Pt 7

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°. ...[more]

PMID: 22750872

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