1aie

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==Overview==
==Overview==
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The molecular replacement method is a powerful technique for crystal, structure solution but the use of NMR structures as templates often causes, problems. In this work the NMR structure of the p53 tetramerization domain, has been used to solve the crystal structure by molecular replacement., Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein, complex was used to identify correct solutions. The three-dimensional, structure of residues 326-356 was subsequently refined to a final R factor, of 19.1% at 1.5 A resolution.
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The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of the p53 tetramerization domain has been used to solve the crystal structure by molecular replacement. Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein complex was used to identify correct solutions. The three-dimensional structure of residues 326-356 was subsequently refined to a final R factor of 19.1% at 1.5 A resolution.
==Disease==
==Disease==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chene, P.]]
[[Category: Chene, P.]]
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[[Category: Gruetter, M.G.]]
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[[Category: Gruetter, M G.]]
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[[Category: Mittl, P.R.E.]]
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[[Category: Mittl, P R.E.]]
[[Category: dna]]
[[Category: dna]]
[[Category: oligomer]]
[[Category: oligomer]]
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[[Category: tumor suppressor]]
[[Category: tumor suppressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:29:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:49 2008''

Revision as of 09:44, 21 February 2008


1aie, resolution 1.5Å

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P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE

Contents

Overview

The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of the p53 tetramerization domain has been used to solve the crystal structure by molecular replacement. Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein complex was used to identify correct solutions. The three-dimensional structure of residues 326-356 was subsequently refined to a final R factor of 19.1% at 1.5 A resolution.

Disease

Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]

About this Structure

1AIE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template., Mittl PR, Chene P, Grutter MG, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9. PMID:9761820

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