Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution.
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.
Nieves-Alicea
R
R
Department of Biochemistry, University of Puerto Rico, Medical Sciences Campus, San Juan, PR 00936-5067, USA.
Focia
P J
PJ
Craig
S P
SP
Eakin
A E
AE
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D003461:Crystallography; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D007041:Hypoxanthine Phosphoribosyltransferase / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009154:Mutation; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014349:Trypanosoma cruzi / Q000201:enzymology*
D010446:Peptide Fragments; D011994:Recombinant Proteins; D007041:Hypoxanthine Phosphoribosyltransferase; D010450:Endopeptidases