Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding.
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| Title: | Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding. |
|---|---|
| Authors: | Mingdong Huang1,2,3, Weissman, Jacques T.1, Chenqian Wang1, Balch, William E.1,2,4 webalch@scripps.edu, Wilson, Lan A.2,5 |
| Source: | Acta Crystallographica: Section D (Wiley-Blackwell). Apr2002, Vol. 58 Issue 4, p700-703. 4p. |
| Subjects: | Protein engineering, Crystallization, Light scattering, Biochemical engineering, Genetic engineering, Guanosine triphosphatase |
| Abstract: | Sar1 is an important and unique GTPase that regulates vesicle budding from the ER membrane. An effort to crystallize full-length hamster Sar1 was unsuccessful owing to the aggregation of Sar1 in solution as indicated by dynamic light-scattering measurements. It was presumed that a patch of hydrophobic residues in the N-terminal region of Sar1 was responsible for the aggregation. To attempt to improve protein crystallizability, the N-terminal residues of Sari were progressively truncated and the solution behavior of the resulting Sari variants was monitored by dynamic light scattering. Truncation of the first nine residues from the N-terminus led to a Sar1 variant that is monodisperse in solution. This well behaved Sari variant yielded crystals in just a few days that were ultimately refined to diffraction quality. [ABSTRACT FROM AUTHOR] |
| Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 14987302 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Mingdong+Huang%22">Mingdong Huang</searchLink><relatesTo>1,2,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Weissman%2C+Jacques+T%2E%22">Weissman, Jacques T.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Chenqian+Wang%22">Chenqian Wang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Balch%2C+William+E%2E%22">Balch, William E.</searchLink><relatesTo>1,2,4</relatesTo><i> webalch@scripps.edu</i><br /><searchLink fieldCode="AR" term="%22Wilson%2C+Lan+A%2E%22">Wilson, Lan A.</searchLink><relatesTo>2,5</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Acta+Crystallographica%3A+Section+D+%28Wiley-Blackwell%29%22">Acta Crystallographica: Section D (Wiley-Blackwell)</searchLink>. Apr2002, Vol. 58 Issue 4, p700-703. 4p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Protein+engineering%22">Protein engineering</searchLink><br /><searchLink fieldCode="DE" term="%22Crystallization%22">Crystallization</searchLink><br /><searchLink fieldCode="DE" term="%22Light+scattering%22">Light scattering</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemical+engineering%22">Biochemical engineering</searchLink><br /><searchLink fieldCode="DE" term="%22Genetic+engineering%22">Genetic engineering</searchLink><br /><searchLink fieldCode="DE" term="%22Guanosine+triphosphatase%22">Guanosine triphosphatase</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Sar1 is an important and unique GTPase that regulates vesicle budding from the ER membrane. An effort to crystallize full-length hamster Sar1 was unsuccessful owing to the aggregation of Sar1 in solution as indicated by dynamic light-scattering measurements. It was presumed that a patch of hydrophobic residues in the N-terminal region of Sar1 was responsible for the aggregation. To attempt to improve protein crystallizability, the N-terminal residues of Sari were progressively truncated and the solution behavior of the resulting Sari variants was monitored by dynamic light scattering. Truncation of the first nine residues from the N-terminus led to a Sar1 variant that is monodisperse in solution. This well behaved Sari variant yielded crystals in just a few days that were ultimately refined to diffraction quality. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=14987302 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1107/S090744490200238X Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 4 StartPage: 700 Subjects: – SubjectFull: Protein engineering Type: general – SubjectFull: Crystallization Type: general – SubjectFull: Light scattering Type: general – SubjectFull: Biochemical engineering Type: general – SubjectFull: Genetic engineering Type: general – SubjectFull: Guanosine triphosphatase Type: general Titles: – TitleFull: Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Mingdong Huang – PersonEntity: Name: NameFull: Weissman, Jacques T. – PersonEntity: Name: NameFull: Chenqian Wang – PersonEntity: Name: NameFull: Balch, William E. – PersonEntity: Name: NameFull: Wilson, Lan A. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 04 Text: Apr2002 Type: published Y: 2002 Identifiers: – Type: issn-print Value: 09074449 Numbering: – Type: volume Value: 58 – Type: issue Value: 4 Titles: – TitleFull: Acta Crystallographica: Section D (Wiley-Blackwell) Type: main |
| ResultId | 1 |
