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Cloning, Expression, Purification, Crystallization and X-Ray Analysis of Inositol Monophosphatase from Mus Musculus and Homo Sapiens

DOI: 10.1107/S1744309112035191 DOI Help
PMID: 23027737 PMID Help

Authors: Nisha Singh (University of Oxford) , Amy C. Halliday (University of Oxford) , Matthew Knight (University of Oxford) , Nathan Lack (Department of Pharmacology, University of Oxford) , Ed Lowe (University of Oxford) , Grant C. Churchill (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 68 (10) , PAGES 1149 - 1152

State: Published (Approved)
Published: October 2012

Abstract: Inositol monophosphatase (IMPase) catalyses the hydrolysis of inositol monophosphate to inositol and is crucial in the phosphatidylinositol (PI) signalling pathway. Lithium, which is the drug of choice for bipolar disorder, inhibits IMPase at therapeutically relevant plasma concentrations. Both mouse IMPase 1 (MmIMPase 1) and human IMPase 1 (HsIMPase 1) were cloned into pRSET5a, expressed in Escherichia coli, purified and crystallized using the sitting-drop method. The structures were solved at resolutions of 2.4 and 1.7 Å, respectively. Comparison of MmIMPase 1 and HsIMPase 1 revealed a core r.m.s. deviation of 0.516 Å.

Journal Keywords: Cloning; Molecular; Crystallization; Crystallography; X-Ray; Gene; Humans; Inositol; Mice; Models; Molecular; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)