A. E. Tishin, A. V. Gladysheva, L. A. Pyatavina, S. E. Olkin, A. A. Gladysheva, I. R. Imatdionov, A. V. Vlaskina, A. Yu. Nikolaeva, V. R. Samygina, A. P. Agafonov
{"title":"鼻病毒 A28 的皮康宁 3C 的制备和结晶","authors":"A. E. Tishin, A. V. Gladysheva, L. A. Pyatavina, S. E. Olkin, A. A. Gladysheva, I. R. Imatdionov, A. V. Vlaskina, A. Yu. Nikolaeva, V. R. Samygina, A. P. Agafonov","doi":"10.1134/s1063774523601119","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.</p>","PeriodicalId":527,"journal":{"name":"Crystallography Reports","volume":null,"pages":null},"PeriodicalIF":0.6000,"publicationDate":"2024-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Preparation and Crystallization of Picornain 3C of Rhinovirus A28\",\"authors\":\"A. E. Tishin, A. V. Gladysheva, L. A. Pyatavina, S. E. Olkin, A. A. Gladysheva, I. R. Imatdionov, A. V. Vlaskina, A. Yu. Nikolaeva, V. R. Samygina, A. P. Agafonov\",\"doi\":\"10.1134/s1063774523601119\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<h3 data-test=\\\"abstract-sub-heading\\\">Abstract</h3><p>Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.</p>\",\"PeriodicalId\":527,\"journal\":{\"name\":\"Crystallography Reports\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.6000,\"publicationDate\":\"2024-02-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Crystallography Reports\",\"FirstCategoryId\":\"88\",\"ListUrlMain\":\"https://doi.org/10.1134/s1063774523601119\",\"RegionNum\":4,\"RegionCategory\":\"材料科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CRYSTALLOGRAPHY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Crystallography Reports","FirstCategoryId":"88","ListUrlMain":"https://doi.org/10.1134/s1063774523601119","RegionNum":4,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CRYSTALLOGRAPHY","Score":null,"Total":0}
Preparation and Crystallization of Picornain 3C of Rhinovirus A28
Abstract
Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.
期刊介绍：
Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
