Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution
1998
Nieves-Alicea, R. | Focia, P.J. | Craig, S.P. III. | Eakin, A.E.
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 angstrom resolution.
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书目信息
Biochimica et biophysica acta = International journal of biochemistry and biophysics
卷
1388
期
2
页码
500
- 505
ISSN
0006-3002
出版者
Elsevier Science
其它主题
X-ray; Crystallography; Crystallography; X-ray diffraction; Crystallography; Peptide fragments; Endopeptidases; Molecular sequence data; Amino acid sequence; Crystal structure; Hypoxanthine phosphoribosyltransferase
语言
英语
注释
2019-12-05
类型
Journal Article; Text
2024-02-27
MODS