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Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens

Research output: Contribution to journalArticle

Nisha Singh, Amy C Halliday, Matthew Knight, Nathan A Lack, Edward Lowe, Grant C Churchill

Original languageEnglish
Pages (from-to)1149-1152
Number of pages4
JournalActa Crystallographica Section F-Structural Biology And Crystallization Communications
Volume68
Issue number10
DOIs
Publication statusPublished - 1 Oct 2012

King's Authors

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.

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