About: Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease
Creator	Gao, Feng Qi, Jianxun Yan, Jinghua Peng, Hao Tian, Kegong Feng, Youjun Jiang, Fan Tian, Xinsheng Zhao, Tiezhu
Source	Medline; PMC
abstract	3CL protease, a viral chymotrypsin-like proteolytic enzyme, plays a pivotal role in the transcription and replication machinery of many RNA viruses, including porcine reproductive and respiratory syndrome virus (PRRSV). In this study, the full-length 3CL protease from PRRSV was cloned and overexpressed in Escherichia coli. Crystallization experiments yielded crystals that diffracted to 2.1 Å resolution and belong to space group C2, with unit-cell parameters a = 112.31, b = 48.34, c = 42.88 Å, β = 109.83°. The Matthews coefficient and the solvent content were calculated to be 2.49 Å(3) Da(−1) and 50.61%, respectively, for one molecule in the asymmetric unit.
has issue date	2007-07-28(xsd:dateTime)
bibo:doi	10.1107/s1744309107033234
bibo:pmid	17671377
has license	green-oa
sha1sum (hex)	2c95e1b07dbd856d0007121257e8435472360888
schema:url	https://doi.org/10.1107/s1744309107033234
resource representing a document's title	Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease
has PubMed Central identifier	PMC2335157
has PubMed identifier	17671377
schema:publication	Acta Crystallographica Section F Structural Biology and Crystallization Communications
resource representing a document's body	covid:2c95e1b07dbd856d0007121257e8435472360888#body_text
is schema:about of	named entity 'space group' named entity 'purification' named entity 'STRUCTURAL BIOLOGY' named entity 'PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS' named entity 'LIKE' named entity 'ESCHERICHIA COLI' named entity 'CRYSTALS' named entity 'PROTEASE' named entity 'ASYMMETRIC' named entity 'LENGTH' named entity 'MATTHEWS' named entity 'ANALYSIS' named entity 'EXPERIMENTS' named entity 'STUDY' named entity '112' named entity 'TRANSCRIPTION' named entity '2.1' named entity 'SOLVENT' named entity 'INCLUDING' named entity 'CRYSTALLIZATION' named entity 'COMMUNICATIONS' named entity 'PURIFICATION' named entity 'VIRAL' named entity 'SPACE GROUP' named entity 'MOLECULAR CLONING' named entity 'PRRSV' named entity 'PROTEOLYTIC ENZYME' named entity 'CRYSTALLIZATION' named entity 'EXPRESSION' named entity 'PLAYS' named entity 'CALCULATED' named entity 'PROTEASE' named entity 'MACHINERY' named entity 'REPLICATION' named entity 'MOLECULE' named entity 'RNA VIRUSES' named entity 'RESOLUTION' named entity 'COEFFICIENT' named entity 'CHYMOTRYPSIN' named entity '2.49' named entity 'CELL' named entity 'PARAMETERS' named entity 'ROLE' named entity 'UNIT' named entity 'CLONED' named entity 'CONTENT' named entity 'protease' named entity 'viral' named entity 'respiratory' named entity 'space group' named entity 'proteolytic enzyme' named entity 'Crystallization' named entity 'Molecular cloning' named entity '3CL protease' named entity 'Porcine reproductive and respiratory syndrome' named entity 'protein' named entity 'PDB' named entity '3CL protease' named entity 'SDS-PAGE' named entity 'X-ray generator' named entity 'protein' named entity 'NaCl' named entity 'ultrafiltration' named entity 'X-rays' named entity 'C-terminal' named entity 'crystal structure' named entity 'primers' named entity '3CL protease' named entity 'C-terminal' named entity 'DTT' named entity 'EAV' named entity 'X-ray diffraction' named entity 'N-terminus'

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