Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase

Robert Serek, Jade Forwood, David Hume, Jennifer L. Martin, B. Kobe

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

The mammalian long-chain acyl-CoA thioesterase, the enzyme that catalyses the hydrolysis of acyl-CoAs to free fatty acids, contains two fused 4HBT (4-­hydroxybenzoyl-CoA thioesterase) motifs. The C-terminal domain of the mouse long-chain acyl-CoA thioesterase (Acot7) has been expressed in bacteria and crystallized. The crystals were obtained by vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 290'K. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82'Ã…, ' = 120°). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4'Ã… resolution using the laboratory X-ray source and are suitable for crystal structure determination.
Original languageEnglish
Pages (from-to)133-135
Number of pages3
JournalActa Crystallographica Section F:Structural Biology Communications
Volume62
Issue number2
DOIs
Publication statusPublished - 2006

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