About: Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli
Creator	Xu, Yue Ito, Kiyoshi Ito, Takashi Nakajima, Yoshitaka Nakashima, Kanako Onohara, Yuko Yoshimoto, Tadashi
Source	Medline; PMC
abstract	A recombinant form of aminopeptidase N (molecular weight 99 kDa) from Escherichia coli was crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitating agent. The crystals belong to the hexagonal space group P3(1)21, with unit-cell parameters a = b = 120.5, c = 171.0 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V (M) value of 3.62 Å(3) Da(−1). Diffraction data were collected to 2.0 Å resolution using Cu Kα radiation from a rotating-anode X-ray generator.
has issue date	2006-06-26(xsd:dateTime)
bibo:doi	10.1107/s1744309106021567
bibo:pmid	16820698
has license	green-oa
sha1sum (hex)	2eab969b4707b77e51678172a746e6ac135014d6
schema:url	https://doi.org/10.1107/s1744309106021567
resource representing a document's title	Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli
has PubMed Central identifier	PMC2242940
has PubMed identifier	16820698
schema:publication	Acta Crystallographica Section F Structural Biology and Crystallization Communications
resource representing a document's body	covid:2eab969b4707b77e51678172a746e6ac135014d6#body_text
is schema:about of	named entity 'Escherichia coli' named entity 'Communications' named entity 'Crystallization' named entity 'PRELIMINARY' named entity 'HANGING' named entity 'FORM' named entity 'SPACE GROUP' named entity 'MOLECULE' named entity 'TO CONTAIN' named entity 'COLLECTED' named entity 'ANODE' named entity 'RADIATION' named entity 'USING' named entity 'ESCHERICHIA COLI' named entity 'RESOLUTION' named entity 'CHARACTERIZATION' named entity 'ASYMMETRIC' named entity 'AMINOPEPTIDASE N' named entity 'AGENT' named entity 'HEXAGONAL' named entity 'CELL' named entity 'WEIGHT' named entity 'VALUE' named entity 'AMMONIUM SULFATE' named entity 'STRUCTURAL BIOLOGY' named entity 'DROP' named entity 'ESCHERICHIA COLI' named entity 'CRYSTALLIZATION' named entity 'AMINOPEPTIDASE N' named entity 'CRYSTALLIZED' named entity '120' named entity 'DIFFRACTION DATA' named entity 'UNIT' named entity 'DIFFUSION METHOD' named entity 'PRECIPITATING' named entity 'MOST LIKELY' named entity 'CRYSTALS' named entity 'COMMUNICATIONS' named entity 'X-RAY' named entity 'RECOMBINANT' named entity 'X-RAY GENERATOR' named entity 'VAPOUR' named entity 'PARAMETERS' named entity 'KDA' named entity 'ROTATING' named entity 'kDa' named entity 'X-ray' named entity 'molecule' named entity 'precipitating agent' named entity 'zinc-binding' named entity 'gene' named entity 'p-chloromercuribenzoate' named entity 'substrate' named entity 'recombinant enzyme' named entity 'precipitate' named entity 'EC 3.4.11.2' named entity 'PstI' named entity 'E. coli' named entity 'N-terminal' named entity 'diffusion' named entity 'ammonium sulfate' named entity 'atom' named entity 'supernatant' named entity 'anode' named entity 'X-ray crystallographic analysis' named entity 'enzyme' named entity 'three-dimensional structure' named entity 'Lys' named entity 'Escherichia coli' named entity 'receptor' named entity 'open reading frame' named entity 'open reading frame' named entity 'molecular weight' named entity 'overexpress' named entity 'zinc ion'

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