Use of transmission electron microscopy to identify nanocrystals of challenging protein targets
Identifieur interne : 000953 ( Main/Exploration ); précédent : 000952; suivant : 000954Use 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 CaleroSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Cellules Sf9, Cristallisation, Cristallographie aux rayons X, Escherichia coli (génétique), Microscopie électronique à transmission (), Nanoparticules (), Nanoparticules (ultrastructure), Protéines (), Protéines (génétique), Protéines (ultrastructure), Protéines recombinantes (), Protéines recombinantes (ultrastructure), Reproductibilité des résultats.
- MESH :
English descriptors
- KwdEn :
- Animals, Crystallization, Crystallography, X-Ray, Escherichia coli (genetics), Microscopy, Electron, Transmission (methods), Nanoparticles (chemistry), Nanoparticles (ultrastructure), Proteins (chemistry), Proteins (genetics), Proteins (ultrastructure), Recombinant Proteins (chemistry), Recombinant Proteins (ultrastructure), Reproducibility of Results, Sf9 Cells.
- MESH :
- chemical , chemistry : Proteins, Recombinant Proteins.
- chemistry : Nanoparticles.
- genetics : Escherichia coli, Proteins.
- methods : Microscopy, Electron, Transmission.
- ultrastructure : Nanoparticles, Proteins, Recombinant Proteins.
- Animals, Crystallization, Crystallography, X-Ray, Reproducibility of Results, Sf9 Cells.
Abstract
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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94305;</nlm:aff>
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<author><name sortKey="Ross, Ted M" sort="Ross, Ted M" uniqKey="Ross T" first="Ted M." last="Ross">Ted M. Ross</name>
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94025;</nlm:aff>
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<term>Crystallography, X-Ray</term>
<term>Escherichia coli (genetics)</term>
<term>Microscopy, Electron, Transmission (methods)</term>
<term>Nanoparticles (chemistry)</term>
<term>Nanoparticles (ultrastructure)</term>
<term>Proteins (chemistry)</term>
<term>Proteins (genetics)</term>
<term>Proteins (ultrastructure)</term>
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<term>Cellules Sf9</term>
<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
<term>Escherichia coli (génétique)</term>
<term>Microscopie électronique à transmission ()</term>
<term>Nanoparticules ()</term>
<term>Nanoparticules (ultrastructure)</term>
<term>Protéines ()</term>
<term>Protéines (génétique)</term>
<term>Protéines (ultrastructure)</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (ultrastructure)</term>
<term>Reproductibilité des résultats</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteins</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanoparticles</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
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</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Microscopy, Electron, Transmission</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanoparticles</term>
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<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
<term>Microscopie électronique à transmission</term>
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<front><div type="abstract" xml:lang="en"><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>
</div>
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<affiliations><list></list>
<tree><noCountry><name sortKey="Barnes, Christopher O" sort="Barnes, Christopher O" uniqKey="Barnes C" first="Christopher O." last="Barnes">Christopher O. Barnes</name>
<name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name>
<name sortKey="Calero, Monica" sort="Calero, Monica" uniqKey="Calero M" first="Monica" last="Calero">Monica Calero</name>
<name sortKey="Cohen, Aina E" sort="Cohen, Aina E" uniqKey="Cohen A" first="Aina E." last="Cohen">Aina E. Cohen</name>
<name sortKey="Conway, James F" sort="Conway, James F" uniqKey="Conway J" first="James F." last="Conway">James F. Conway</name>
<name sortKey="Edwards, Andrea L" sort="Edwards, Andrea L" uniqKey="Edwards A" first="Andrea L." last="Edwards">Andrea L. Edwards</name>
<name sortKey="Khosla, Chaitan" sort="Khosla, Chaitan" uniqKey="Khosla C" first="Chaitan" last="Khosla">Chaitan Khosla</name>
<name sortKey="Lin, Guowu" sort="Lin, Guowu" uniqKey="Lin G" first="Guowu" last="Lin">Guowu Lin</name>
<name sortKey="Makhov, Alexander M" sort="Makhov, Alexander M" uniqKey="Makhov A" first="Alexander M." last="Makhov">Alexander M. Makhov</name>
<name sortKey="Mathews, Irimpan I" sort="Mathews, Irimpan I" uniqKey="Mathews I" first="Irimpan I." last="Mathews">Irimpan I. Mathews</name>
<name sortKey="Nagarajan, V" sort="Nagarajan, V" uniqKey="Nagarajan V" first="V." last="Nagarajan">V. Nagarajan</name>
<name sortKey="Ross, Ted M" sort="Ross, Ted M" uniqKey="Ross T" first="Ted M." last="Ross">Ted M. Ross</name>
<name sortKey="Santamaria, Hugo" sort="Santamaria, Hugo" uniqKey="Santamaria H" first="Hugo" last="Santamaria">Hugo Santamaria</name>
<name sortKey="Soltis, S Michael" sort="Soltis, S Michael" uniqKey="Soltis S" first="S. Michael" last="Soltis">S. Michael Soltis</name>
<name sortKey="Stevenson, Hilary P" sort="Stevenson, Hilary P" uniqKey="Stevenson H" first="Hilary P." last="Stevenson">Hilary P. Stevenson</name>
<name sortKey="Zeldin, Oliver B" sort="Zeldin, Oliver B" uniqKey="Zeldin O" first="Oliver B." last="Zeldin">Oliver B. Zeldin</name>
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