Sensitivity boosts by the CPMAS CryoProbe for challenging biological assemblies.


Journal

Journal of magnetic resonance (San Diego, Calif. : 1997)
ISSN: 1096-0856
Titre abrégé: J Magn Reson
Pays: United States
ID NLM: 9707935

Informations de publication

Date de publication:
02 2020
Historique:
received: 25 09 2019
revised: 19 12 2019
accepted: 21 12 2019
pubmed: 18 1 2020
medline: 10 7 2021
entrez: 18 1 2020
Statut: ppublish

Résumé

Despite breakthroughs in MAS NMR hardware and experimental methodologies, sensitivity remains a major challenge for large and complex biological systems. Here, we report that 3-4 fold higher sensitivities can be obtained in heteronuclear-detected experiments, using a novel HCN CPMAS probe, where the sample coil and the electronics operate at cryogenic temperatures, while the sample is maintained at ambient temperatures (BioSolids CryoProbe™). Such intensity enhancements permit recording 2D and 3D experiments that are otherwise time-prohibitive, such as 2D

Identifiants

pubmed: 31951864
pii: S1090-7807(19)30319-2
doi: 10.1016/j.jmr.2019.106680
pmc: PMC7060763
mid: NIHMS1550443
pii:
doi:

Substances chimiques

Capsid Proteins 0
Indicators and Reagents 0
KIF5B protein, human 0
Prion Proteins 0
Hydrogen Cyanide 2WTB3V159F
Carbon 7440-44-0
Kinesins EC 3.6.4.4

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

106680

Subventions

Organisme : NIGMS NIH HHS
ID : P30 GM110758
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM123743
Pays : United States
Organisme : NIAID NIH HHS
ID : P50 AI150481
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG061797
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM094357
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Références

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Auteurs

Alia Hassan (A)

Bruker Biospin Corporation, Fällanden, Switzerland. Electronic address: Alia.Hassan@bruker.com.

Caitlin M Quinn (CM)

Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, United States.

Jochem Struppe (J)

Bruker Biospin Corporation, 15 Fortune Drive, Billerica, MA, United States.

Ivan V Sergeyev (IV)

Bruker Biospin Corporation, 15 Fortune Drive, Billerica, MA, United States.

Chunting Zhang (C)

Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, United States.

Changmiao Guo (C)

Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, United States.

Brent Runge (B)

Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States.

Theint Theint (T)

Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, United States.

Hanh H Dao (HH)

Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, United States.

Christopher P Jaroniec (CP)

Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, United States.

Mélanie Berbon (M)

CNRS, CBMN, UMR5248, University of Bordeaux, F-33600 Pessac, France.

Alons Lends (A)

CNRS, CBMN, UMR5248, University of Bordeaux, F-33600 Pessac, France.

Birgit Habenstein (B)

CNRS, CBMN, UMR5248, University of Bordeaux, F-33600 Pessac, France.

Antoine Loquet (A)

CNRS, CBMN, UMR5248, University of Bordeaux, F-33600 Pessac, France.

Rainer Kuemmerle (R)

Bruker Biospin Corporation, Fällanden, Switzerland.

Barbara Perrone (B)

Bruker Biospin Corporation, Fällanden, Switzerland. Electronic address: barbara.perrone@bruker.com.

Angela M Gronenborn (AM)

Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States; Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Ave., Pittsburgh, PA, United States. Electronic address: amg100@pitt.edu.

Tatyana Polenova (T)

Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, United States; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States. Electronic address: tpolenov@udel.edu.

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