Highest impact structures: Difference between revisions
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===20th Century=== | ===20th Century=== | ||
* '''1953 - [[DNA]] double helix''' (B form): Although Watson and Crick's model was theoretical | * '''1953 - [[DNA]] double helix''' (B form): Although Watson and Crick's model was not based on 3D crystallographic data, the fiber diffraction images obtained by Rosalind Franklin guided them in their hypotheses. The theoretical model they arrived at was essentially correct, and for the first time explained the ability of genes to be faithfully copied during cell division. It was not confirmed by atomic resolution X-ray crystallography until 1973, using RNA dinucleotide crystals. A full turn of B form DNA was not solved until 1980 (cf. [[1bna]]), 27 years after Watson and Crick's model. More: click on DNA at the [http://atlas.molviz.org Atlas of Macromolecules] | ||
* '''1958 - [[Myoglobin]]''': As the first protein structure that was determined, it is hard to exaggerate its impact. Before this structure, proteins were widely believed to be colloidal, and protein crystals were expected to contain highly symmetrical structures. The irregular fold of myoglobin (see photo of an early low-resolution model at [[Nobel Prizes for 3D Molecular Structure]]) was a huge surprise. | * '''1958 - [[Myoglobin]]''': As the first protein structure that was determined, it is hard to exaggerate its impact. Before this structure, proteins were widely believed to be colloidal, and protein crystals were expected to contain highly symmetrical structures. The irregular fold of myoglobin (see photo of an early low-resolution model at [[Nobel Prizes for 3D Molecular Structure]]) was a huge surprise. | ||
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* '''2007 and 2011 - [[G protein-coupled receptor]]''': In 2007 the structure of the first ligand-activated G protein-coupled receptor and in 2011 the first activated G protein-coupled receptor bound to its G protein. This is a large class of proteins that have great importance as targets for drug development; it is estimated that 4% of the human genome devoted to protein coding encodes this class of proteins. The determination of the structures lead to Brian Kobilika sharing the [[Nobel_Prizes_for_3D_Molecular_Structure#Twenty-First_Century|2012 Nobel Prize in Chemistry]] | * '''2007 and 2011 - [[G protein-coupled receptor]]''': In 2007 the structure of the first ligand-activated G protein-coupled receptor and in 2011 the first activated G protein-coupled receptor bound to its G protein. This is a large class of proteins that have great importance as targets for drug development; it is estimated that 4% of the human genome devoted to protein coding encodes this class of proteins. The determination of the structures lead to Brian Kobilika sharing the [[Nobel_Prizes_for_3D_Molecular_Structure#Twenty-First_Century|2012 Nobel Prize in Chemistry]] | ||
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* '''2019 - Cytochrome nanowires''': [[6ef8]] was the first structure of an electrically-conductive bacterial protein nanowire, confirmed by [[6nef]]. Such nanowires appear to be important in global carbon and metal redox phenomena in anoxic soils and sediments, and have many possible applications<ref>PMID: 24863901</ref><ref>PMID:27801905</ref><ref>PMID: 31240257</ref>. Prior to these [[cryo-EM]] structures, it had been believed for over a decade that nanowires were type IV pili assembled from pilA<ref>PMID: 30951668</ref>. These structures surprisingly revealed nanowires as polymers of 6-heme C-type cytochromes, which called this belief into question. The unexpected protein making up these nanowires was determined from the cryo-EM density map. This is an unusual case in which the protein making up an extensively-studied organelle was not known prior to solving its atomic-level structure. | * '''2019 - Cytochrome nanowires''': [[6ef8]] was the first structure of an electrically-conductive bacterial protein nanowire, confirmed by [[6nef]]. Such nanowires appear to be important in global carbon and metal redox phenomena in anoxic soils and sediments, and have many possible applications<ref>PMID: 24863901</ref><ref>PMID:27801905</ref><ref>PMID: 31240257</ref>. Prior to these [[cryo-EM]] structures, it had been believed for over a decade that nanowires were type IV pili assembled from pilA<ref>PMID: 30951668</ref>. These structures surprisingly revealed nanowires as polymers of 6-heme C-type cytochromes, which called this belief into question. The unexpected protein making up these nanowires was determined from the cryo-EM density map. This is an unusual case in which the protein making up an extensively-studied organelle was not known prior to solving its atomic-level structure. | ||
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==Structures Saving The Most Lives== | ==Structures Saving The Most Lives== | ||
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*[http://www.umass.edu/microbio/rasmol/1st_xtls.htm Earliest Solutions for Macromolecular Crystal Structures] | *[http://www.umass.edu/microbio/rasmol/1st_xtls.htm Earliest Solutions for Macromolecular Crystal Structures] | ||
*[[Personal favorites]] | *[[Personal favorites]] | ||
* [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3945011/ Biophysical Highlights from 54 Years of Macromolecular Crystallography, Richardson and Richardson], a 2014 review in ''Biophysical Journal''. | |||
*[http://www.molecularstructure.org/ Structural Biology Rankings] ranks 3D structures according to their popularity among scientists and citation count. | *[http://www.molecularstructure.org/ Structural Biology Rankings] ranks 3D structures according to their popularity among scientists and citation count. | ||
