Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution

René Nieves-Alicea; Pamela J. Focia; Sydney P. Craig; Ann E. Eakin

doi:10.1016/S0167-4838(98)00210-6

Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution

René Nieves-Alicea, Pamela J. Focia, Sydney P. Craig, Ann E. Eakin^*

^*Corresponding author for this work

Biochemistry and Molecular Genetics

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

9 Scopus citations

Abstract

Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution. Copyright (C) 1998 Elsevier Science B.V.

Original language	English (US)
Pages (from-to)	500-505
Number of pages	6
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1388
Issue number	2
DOIs	https://doi.org/10.1016/S0167-4838(98)00210-6
State	Published - Nov 10 1998

Funding

We are grateful to Robert Stevens of the Mass Spectrometry Facility of the Duke University Medical Center for the ES-MS data and to Astrid Guerra for technical assistance. This project was granted synchrotron beamline access (program proposal number 4A16) by the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the DOE and NIH. This work was supported in part by NIH Grants AI38919 (to A.E.E.), AI34326 (to S.P.C. III) and RR03051. R.N.-A. was supported by a fellowship from the Ford Foundation.

Keywords

Crystallization
Electro-spray mass spectrometry
Hypoxanthine phosphoribosyltransferase
Limited proteolysis
Parasite
Trypanosoma

ASJC Scopus subject areas

Molecular Biology
Structural Biology
Biophysics
Biochemistry

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10.1016/S0167-4838(98)00210-6

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title = "Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution",

abstract = "Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution. Copyright (C) 1998 Elsevier Science B.V.",

keywords = "Crystallization, Electro-spray mass spectrometry, Hypoxanthine phosphoribosyltransferase, Limited proteolysis, Parasite, Trypanosoma",

author = "Ren{\'e} Nieves-Alicea and Focia, {Pamela J.} and Craig, {Sydney P.} and Eakin, {Ann E.}",

note = "Funding Information: We are grateful to Robert Stevens of the Mass Spectrometry Facility of the Duke University Medical Center for the ES-MS data and to Astrid Guerra for technical assistance. This project was granted synchrotron beamline access (program proposal number 4A16) by the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the DOE and NIH. This work was supported in part by NIH Grants AI38919 (to A.E.E.), AI34326 (to S.P.C. III) and RR03051. R.N.-A. was supported by a fellowship from the Ford Foundation.",

year = "1998",

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doi = "10.1016/S0167-4838(98)00210-6",

language = "English (US)",

volume = "1388",

pages = "500--505",

journal = "Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology",

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Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution. / Nieves-Alicea, René; Focia, Pamela J.; Craig, Sydney P. et al.
In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1388, No. 2, 10.11.1998, p. 500-505.

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

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T1 - Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution

AU - Nieves-Alicea, René

AU - Focia, Pamela J.

AU - Craig, Sydney P.

AU - Eakin, Ann E.

N1 - Funding Information: We are grateful to Robert Stevens of the Mass Spectrometry Facility of the Duke University Medical Center for the ES-MS data and to Astrid Guerra for technical assistance. This project was granted synchrotron beamline access (program proposal number 4A16) by the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the DOE and NIH. This work was supported in part by NIH Grants AI38919 (to A.E.E.), AI34326 (to S.P.C. III) and RR03051. R.N.-A. was supported by a fellowship from the Ford Foundation.

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N2 - Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution. Copyright (C) 1998 Elsevier Science B.V.

AB - Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution. Copyright (C) 1998 Elsevier Science B.V.

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KW - Limited proteolysis

KW - Parasite

KW - Trypanosoma

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Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution

Abstract

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Keywords

ASJC Scopus subject areas

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