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Open Access Green as soon as Postprint is submitted to ZB.
Purification, crystallization and preliminary crystallographic analysis of the globular domain of the human type V myosin Myo5a.
Acta Crystallogr. F-Struct. Biol. Cryst. Commun. 69, 1220-1223 (2013)
Type V myosins constitute the main cargo-transporting class of myosin motors in higher eukaryotes. They are mainly defined by their C-terminal globular domain, which is required for cargo binding as well as for motor auto-inhibition in the absence of cargo. To date, high-resolution structures only exist for globular domains from yeast. Since the majority of cellular cargoes in yeast are very different from the cargoes in higher eukaryotes, structural insights into the domain organization of globular domains from human type V myosins are important. The globular domain of human Myo5a was cloned, expressed and crystallized and data sets were collected. The crystals belonged to space group P212121, with unit-cell parameters a = 75.04, b = 86.70, c = 131.41 Å, α = β = γ = 90°, and diffracted with data-collection quality to 2.5 Å resolution.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cargo Binding ; Cellular Transport ; Type V Myosin; Crystals ; Disease ; Tail
e-ISSN
2053-230X
Journal
Acta Crystallographica Section F
Quellenangaben
Volume: 69,
Issue: 11,
Pages: 1220-1223
Publisher
Blackwell
Publishing Place
Oxford [u.a.]
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)