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

doi:10.1002/(SICI)1097-0134(199707)28:3<452::AID-PROT13>3.0.CO;2-G

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

Biochemistry

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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 language	English (US)
Pages (from-to)	452-453
Number of pages	2
Journal	Proteins: Structure, Function and Genetics
Volume	28
Issue number	3
DOIs	https://doi.org/10.1002/(SICI)1097-0134(199707)28:3<452::AID-PROT13>3.0.CO;2-G
State	Published - 1997

Keywords

Actin binding
Crystallography
F-actin crosslinker
Fimbrin

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/(SICI)1097-0134(199707)28:3<452::AID-PROT13>3.0.CO;2-G

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title = "Crystallization and preliminary crystallographic analysis of the N- terminal actin binding domain of human fimbrin",

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 {\AA}, b = 61.24 {\AA}, c = 102.30 {\AA}). These crystals contain one molecule in the asymmetric unit and diffract to at least 1.9 {\AA} resolution. The crystal structure of ABD1 will be the first structure of an actin crosslinking domain.",

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year = "1997",

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T1 - Crystallization and preliminary crystallographic analysis of the N- terminal actin binding domain of human fimbrin

AU - Goldsmith, Sharon C.

AU - Pokala, Navin

AU - Matsudaira, Paul

AU - Almo, Steven C.

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

KW - Actin binding

KW - Crystallography

KW - F-actin crosslinker

KW - Fimbrin

UR - https://www.scopus.com/pages/publications/0030986888

UR - https://www.scopus.com/pages/publications/0030986888#tab=citedBy

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DO - 10.1002/(SICI)1097-0134(199707)28:3<452::AID-PROT13>3.0.CO;2-G

M3 - Article

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AN - SCOPUS:0030986888

SN - 0887-3585

VL - 28

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JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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