Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.
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| Title: | Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein. |
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| Authors: | Geerds C; Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany., Niemann HH; Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany. |
| Source: | Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2026 Jan 01; Vol. 82 (Pt 1), pp. 4-13. Date of Electronic Publication: 2026 Jan 01. |
| Publication Type: | Journal Article |
| Journal Info: | Publisher: John Wiley & Sons Inc Country of Publication: United States NLM ID: 101620319 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2053-230X (Electronic) Linking ISSN: 2053230X NLM ISO Abbreviation: Acta Crystallogr F Struct Biol Commun Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
| FullText | Text: Availability: 0 |
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| Header | DbId: mdl DbLabel: MEDLINE Ultimate An: 41324409 AccessLevel: 2 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Geerds+C%22">Geerds C</searchLink>; Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany.<br /><searchLink fieldCode="AU" term="%22Niemann+HH%22">Niemann HH</searchLink>; Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany. – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22101620319%22">Acta crystallographica. Section F, Structural biology communications</searchLink> [Acta Crystallogr F Struct Biol Commun] 2026 Jan 01; Vol. 82 (Pt 1), pp. 4-13. <i>Date of Electronic Publication: </i>2026 Jan 01. – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22John+Wiley+%26+Sons+Inc%22">John Wiley & Sons Inc </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101620319 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>2053-230X (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%222053230X%22">2053230X </searchLink><i>NLM ISO Abbreviation: </i>Acta Crystallogr F Struct Biol Commun <i>Subsets: </i>MEDLINE |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=41324409 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1107/S2053230X25010416 Languages: – Code: eng Text: English PhysicalDescription: Pagination: StartPage: 4 Titles: – TitleFull: Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Geerds C – PersonEntity: Name: NameFull: Niemann HH IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 01 Text: 2026 Jan 01 Type: published Y: 2026 Identifiers: – Type: issn-electronic Value: 2053-230X Numbering: – Type: volume Value: 82 – Type: issue Value: Pt 1 Titles: – TitleFull: Acta crystallographica. Section F, Structural biology communications Type: main |
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