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Crystallization and...
Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain
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- Addario, Barbara (författare)
- Umeå universitet,Kemiska institutionen,Lars Backman
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- Huang, Shenghua (författare)
- Umeå universitet,Kemiska institutionen
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- Sauer, Uwe (författare)
- Umeå universitet,Kemiska institutionen
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- Backman, Lars (författare)
- Umeå universitet,Kemiska institutionen
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(creator_code:org_t)
- International Union of Crystallography, 2011
- 2011
- Engelska.
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Ingår i: Acta Crystallographica. Section F. - : International Union of Crystallography. - 1744-3091 .- 1744-3091. ; 67:10, s. 1214-1217
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- -Actinins form antiparallel homodimers that are able to cross-link actin filaments. The protein contains three domains: an N-terminal actin-binding domain followed by a central rod domain and a calmodulin-like EF-hand domain at the C-terminus. Here, crystallization of the rod domain of Entamoeba histolytica -actinin-2 is reported; it crystallized in space group P212121, with unit-cell parameters a = 47.8, b = 79.1, c = 141.8 Å. A Matthews coefficient VM of 2.6 Å3 Da-1 suggests that there are two molecules and 52.5% solvent content in the asymmetric unit. A complete native data set extending to a d-spacing of 2.8 Å was collected on beamline I911-2 at MAX-lab, Sweden.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- actinin
- Entamoeba histolytica
- actin-binding proteins
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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