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Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain.

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Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain. / Degenhardt, M; Weber, Wolfgang; Eschenburg, S; Dierks, K; Funari, S S; Rapp, G; Betzel, C.

In: ACTA CRYSTALLOGR D, Vol. 54, No. Pt 5, Pt 5, 1998, p. 999-1001.

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

Harvard

Degenhardt, M, Weber, W, Eschenburg, S, Dierks, K, Funari, SS, Rapp, G & Betzel, C 1998, 'Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain.', ACTA CRYSTALLOGR D, vol. 54, no. Pt 5, Pt 5, pp. 999-1001. <http://www.ncbi.nlm.nih.gov/pubmed/9757119?dopt=Citation>

APA

Degenhardt, M., Weber, W., Eschenburg, S., Dierks, K., Funari, S. S., Rapp, G., & Betzel, C. (1998). Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain. ACTA CRYSTALLOGR D, 54(Pt 5), 999-1001. [Pt 5]. http://www.ncbi.nlm.nih.gov/pubmed/9757119?dopt=Citation

Vancouver

Degenhardt M, Weber W, Eschenburg S, Dierks K, Funari SS, Rapp G et al. Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain. ACTA CRYSTALLOGR D. 1998;54(Pt 5):999-1001. Pt 5.

Bibtex

@article{586a08a5ba474e4fbe9329bedc395411,
title = "Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain.",
abstract = "Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor has been accomplished in the presence of the ligand EGF. Two different crystal forms have been obtained, one of which was suitable for X-ray analysis. The space group of this form has been assigned to P21212 with unit-cell dimensions of a = 207.4, b = 113.3 and c = 120.4 A. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these crystals, however, is limited to low resolution and extensive trials to improve crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angle X-ray diffraction and dynamic light-scattering techniques have been applied. Synchrotron radiation in combination with cryo-techniques is essential for data collection because of the high solvent content and radiation sensitivity.",
keywords = "Animals, Mice, Light, Scattering, Radiation, Crystallization, Crystallography, X-Ray/methods, Peptide Fragments/*chemistry/isolation & purification, *Protein Conformation, Receptor, Epidermal Growth Factor/*chemistry/isolation & purification, Animals, Mice, Light, Scattering, Radiation, Crystallization, Crystallography, X-Ray/methods, Peptide Fragments/*chemistry/isolation & purification, *Protein Conformation, Receptor, Epidermal Growth Factor/*chemistry/isolation & purification",
author = "M Degenhardt and Wolfgang Weber and S Eschenburg and K Dierks and Funari, {S S} and G Rapp and C Betzel",
year = "1998",
language = "English",
volume = "54",
pages = "999--1001",
journal = "ACTA CRYSTALLOGR D",
issn = "2059-7983",
publisher = "John Wiley and Sons Inc.",
number = "Pt 5",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain.

AU - Degenhardt, M

AU - Weber, Wolfgang

AU - Eschenburg, S

AU - Dierks, K

AU - Funari, S S

AU - Rapp, G

AU - Betzel, C

PY - 1998

Y1 - 1998

N2 - Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor has been accomplished in the presence of the ligand EGF. Two different crystal forms have been obtained, one of which was suitable for X-ray analysis. The space group of this form has been assigned to P21212 with unit-cell dimensions of a = 207.4, b = 113.3 and c = 120.4 A. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these crystals, however, is limited to low resolution and extensive trials to improve crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angle X-ray diffraction and dynamic light-scattering techniques have been applied. Synchrotron radiation in combination with cryo-techniques is essential for data collection because of the high solvent content and radiation sensitivity.

AB - Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor has been accomplished in the presence of the ligand EGF. Two different crystal forms have been obtained, one of which was suitable for X-ray analysis. The space group of this form has been assigned to P21212 with unit-cell dimensions of a = 207.4, b = 113.3 and c = 120.4 A. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these crystals, however, is limited to low resolution and extensive trials to improve crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angle X-ray diffraction and dynamic light-scattering techniques have been applied. Synchrotron radiation in combination with cryo-techniques is essential for data collection because of the high solvent content and radiation sensitivity.

KW - Animals

KW - Mice

KW - Light

KW - Scattering, Radiation

KW - Crystallization

KW - Crystallography, X-Ray/methods

KW - Peptide Fragments/chemistry/isolation & purification

KW - Protein Conformation

KW - Receptor, Epidermal Growth Factor/chemistry/isolation & purification

KW - Animals

KW - Mice

KW - Light

KW - Scattering, Radiation

KW - Crystallization

KW - Crystallography, X-Ray/methods

KW - Peptide Fragments/chemistry/isolation & purification

KW - Protein Conformation

KW - Receptor, Epidermal Growth Factor/chemistry/isolation & purification

M3 - SCORING: Journal article

VL - 54

SP - 999

EP - 1001

JO - ACTA CRYSTALLOGR D

JF - ACTA CRYSTALLOGR D

SN - 2059-7983

IS - Pt 5

M1 - Pt 5

ER -