Expression, purification and crystallization of human prolylcarboxypeptidase

التفاصيل البيبلوغرافية
العنوان: Expression, purification and crystallization of human prolylcarboxypeptidase
المؤلفون: Rachael E. Ford, Ranabir SinhaRoy, Wayne M. Geissler, Sujata Sharma, Keith W. Rickert, Pravien D. Abeywickrema, Noel Byrne, Kelly Ann D. Pryor, John C. Reid, Dawn L. Hall, Ronald E. Diehl, Kevin J. Lumb, Stephen M. Soisson, Jennifer M. Shipman, Sangita B. Patel
المصدر: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:702-705
بيانات النشر: International Union of Crystallography (IUCr), 2010.
سنة النشر: 2010
مصطلحات موضوعية: Glycosylation, genetic structures, Biophysics, Gene Expression, macromolecular substances, CHO Cells, Carboxypeptidases, Crystallography, X-Ray, Biochemistry, law.invention, chemistry.chemical_compound, Cricetulus, Structural Biology, law, Cricetinae, Gene expression, Genetics, Animals, Humans, Proline, Crystallization, chemistry.chemical_classification, biology, Chinese hamster ovary cell, Condensed Matter Physics, biology.organism_classification, Carboxypeptidase, Amino acid, chemistry, Crystallization Communications, biology.protein
الوصف: Prolylcarboxypeptidase (PrCP) is a lysosomal serine carboxypeptidase that cleaves a variety of C-terminal amino acids adjacent to proline and has been implicated in diseases such as hypertension and obesity. Here, the robust production, purification and crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yielded crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffracted to better than 2.8 A resolution.
تدمد: 1744-3091
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::229e62345941a56cbba4e81a38f08a0f
https://doi.org/10.1107/s1744309110014041
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....229e62345941a56cbba4e81a38f08a0f
قاعدة البيانات: OpenAIRE