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Use of transmission electron microscopy to identify nanocrystals of challenging protein targets

Identifieur interne : 000953 ( Main/Exploration ); précédent : 000952; suivant : 000954

Use of transmission electron microscopy to identify nanocrystals of challenging protein targets

Auteurs : Hilary P. Stevenson ; Alexander M. Makhov ; Monica Calero ; Andrea L. Edwards ; Oliver B. Zeldin ; Irimpan I. Mathews ; Guowu Lin ; Christopher O. Barnes ; Hugo Santamaria ; Ted M. Ross ; S. Michael Soltis ; Chaitan Khosla ; V. Nagarajan ; James F. Conway ; Aina E. Cohen ; Guillermo Calero

Source :

RBID : PMC:4060711

Descripteurs français

English descriptors

Abstract

Significance

X-ray crystallography is the primary technique used to obtain high-resolution structures of proteins. This method relies on diffracting large crystals that are identified by bright-field microscopy and usually optimized from an initial smaller and lower quality crystalline hit. Because of the limits of the optical methods used to visualize and identify these crystals, smaller nanometer crystals are excluded from the results of typical evaluations. However, the field of nanocrystallography, which utilizes a free electron laser to solve structures from nanocrystal (NC) slurries, makes these unidentified crystals highly useful. This paper presents a method, relying on transmission electron microscopy, to identify NCs, determine if they are protein, and evaluate their quality.


Url:
DOI: 10.1073/pnas.1400240111
PubMed: 24872454
PubMed Central: 4060711


Affiliations:


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Le document en format XML

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<term>Microscopy, Electron, Transmission (methods)</term>
<term>Nanoparticles (chemistry)</term>
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<term>Proteins (chemistry)</term>
<term>Proteins (genetics)</term>
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<title>Significance</title>
<p>X-ray crystallography is the primary technique used to obtain high-resolution structures of proteins. This method relies on diffracting large crystals that are identified by bright-field microscopy and usually optimized from an initial smaller and lower quality crystalline hit. Because of the limits of the optical methods used to visualize and identify these crystals, smaller nanometer crystals are excluded from the results of typical evaluations. However, the field of nanocrystallography, which utilizes a free electron laser to solve structures from nanocrystal (NC) slurries, makes these unidentified crystals highly useful. This paper presents a method, relying on transmission electron microscopy, to identify NCs, determine if they are protein, and evaluate their quality.</p>
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