Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

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Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein. / Dar, Imran; Bonny, Christophe; Pedersen, Jan Torleif; Gajhede, Michael; Kristensen, Ole.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 59, No. Pt 12, 2003, p. 2300-2.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Dar, I, Bonny, C, Pedersen, JT, Gajhede, M & Kristensen, O 2003, 'Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein', Acta Crystallographica. Section D: Biological Crystallography, vol. 59, no. Pt 12, pp. 2300-2. https://doi.org/10.1107/S0907444903020304

APA

Dar, I., Bonny, C., Pedersen, J. T., Gajhede, M., & Kristensen, O. (2003). Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein. Acta Crystallographica. Section D: Biological Crystallography, 59(Pt 12), 2300-2. https://doi.org/10.1107/S0907444903020304

Vancouver

Dar I, Bonny C, Pedersen JT, Gajhede M, Kristensen O. Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein. Acta Crystallographica. Section D: Biological Crystallography. 2003;59(Pt 12):2300-2. https://doi.org/10.1107/S0907444903020304

Author

Dar, Imran ; Bonny, Christophe ; Pedersen, Jan Torleif ; Gajhede, Michael ; Kristensen, Ole. / Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein. In: Acta Crystallographica. Section D: Biological Crystallography. 2003 ; Vol. 59, No. Pt 12. pp. 2300-2.

Bibtex

@article{493172ca39824e5f922a9e4894c0ecbb,

title = "Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein",

abstract = "IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.",

keywords = "Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains",

author = "Imran Dar and Christophe Bonny and Pedersen, {Jan Torleif} and Michael Gajhede and Ole Kristensen",

year = "2003",

doi = "10.1107/S0907444903020304",

language = "English",

volume = "59",

pages = "2300--2",

journal = "Acta Crystallographica Section D: Structural Biology",

issn = "2059-7983",

publisher = "International Union of Crystallography",

number = "Pt 12",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

AU - Dar, Imran

AU - Bonny, Christophe

AU - Pedersen, Jan Torleif

AU - Gajhede, Michael

AU - Kristensen, Ole

PY - 2003

Y1 - 2003

N2 - IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.

AB - IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Nuclear Proteins

KW - Recombinant Fusion Proteins

KW - Selenomethionine

KW - Trans-Activators

KW - src Homology Domains

U2 - 10.1107/S0907444903020304

DO - 10.1107/S0907444903020304

M3 - Journal article

C2 - 14646101

VL - 59

SP - 2300

EP - 2302

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 12

ER -

ID: 40318661