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Updated: May 20, 2026
Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Expression, purification, crystallization and preliminary X-ray analysis of the human NORE1 SARAH domain
Hye Jin Kim1, Eunha Hwang, Young-Hyun Han
1Division of Magnetic Resonance, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang, Chungbuk 363-883, Republic of Korea.
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°.
