Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

Cynthia L. Phillips; Buddy Ullman; Richard G. Brennan

doi:10.1002/prot.11

Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

Cynthia L. Phillips, Buddy Ullman, Richard G. Brennan

Biochemistry & Molecular Biology

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

5 Scopus citations

Abstract

Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg²⁺ -α- D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5- monophosphate, as well as in the absence of ligand. These crystals belong to the space group P6₁22 or its enantiomorph P6₅22, with unit cell dimensions of a = b = 64.0 Å, c = 240.5 Å, α = β = 90°, and γ = 120°. The crystals diffract to 1.9 Å.

Original language	English (US)
Pages (from-to)	510-513
Number of pages	4
Journal	Proteins: Structure, Function and Genetics
Volume	25
Issue number	4
DOIs	https://doi.org/10.1002/prot.11
State	Published - 1996

Keywords

Leishmania
X-ray diffraction
parasite metabolism
selenomethionine

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.11

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title = "Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase",

abstract = "Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg2+ -α- D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5- monophosphate, as well as in the absence of ligand. These crystals belong to the space group P6122 or its enantiomorph P6522, with unit cell dimensions of a = b = 64.0 {\AA}, c = 240.5 {\AA}, α = β = 90°, and γ = 120°. The crystals diffract to 1.9 {\AA}.",

keywords = "Leishmania, X-ray diffraction, parasite metabolism, selenomethionine",

author = "Phillips, {Cynthia L.} and Buddy Ullman and Brennan, {Richard G.}",

year = "1996",

doi = "10.1002/prot.11",

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volume = "25",

pages = "510--513",

journal = "Proteins: Structure, Function and Genetics",

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T1 - Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

AU - Phillips, Cynthia L.

AU - Ullman, Buddy

AU - Brennan, Richard G.

PY - 1996

Y1 - 1996

N2 - Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg2+ -α- D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5- monophosphate, as well as in the absence of ligand. These crystals belong to the space group P6122 or its enantiomorph P6522, with unit cell dimensions of a = b = 64.0 Å, c = 240.5 Å, α = β = 90°, and γ = 120°. The crystals diffract to 1.9 Å.

AB - Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg2+ -α- D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5- monophosphate, as well as in the absence of ligand. These crystals belong to the space group P6122 or its enantiomorph P6522, with unit cell dimensions of a = b = 64.0 Å, c = 240.5 Å, α = β = 90°, and γ = 120°. The crystals diffract to 1.9 Å.

KW - Leishmania

KW - X-ray diffraction

KW - parasite metabolism

KW - selenomethionine

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DO - 10.1002/prot.11

M3 - Article

C2 - 8865346

AN - SCOPUS:0029817553

SN - 0887-3585

VL - 25

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JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 4

ER -

Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

Abstract

Keywords

ASJC Scopus subject areas

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