Crystallization and preliminary crystallographic analysis of the N- terminal actin binding domain of human fimbrin

Sharon C. Goldsmith, Navin Pokala, Paul Matsudaira, Steven C. Almo

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

We have crystallized the N-terminal actin binding domain (ABD1) of human fimbrin, a representative member of the largest class of actin crosslinking proteins. Diffraction from these crystals is consistent with the orthorhombic space group P212121 (α = 50.03 Å, b = 61.24 Å, c = 102.30 Å). These crystals contain one molecule in the asymmetric unit and diffract to at least 1.9 Å resolution. The crystal structure of ABD1 will be the first structure of an actin crosslinking domain.

Original languageEnglish (US)
Pages (from-to)452-453
Number of pages2
JournalProteins: Structure, Function and Genetics
Volume28
Issue number3
DOIs
StatePublished - 1997

Fingerprint

Crystallization
Actins
Crosslinking
Crystals
Diffraction
Crystal structure
Molecules
plastin
Proteins

Keywords

  • Actin binding
  • Crystallography
  • F-actin crosslinker
  • Fimbrin

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Crystallization and preliminary crystallographic analysis of the N- terminal actin binding domain of human fimbrin. / Goldsmith, Sharon C.; Pokala, Navin; Matsudaira, Paul; Almo, Steven C.

In: Proteins: Structure, Function and Genetics, Vol. 28, No. 3, 1997, p. 452-453.

Research output: Contribution to journalArticle

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