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  Trapping intermediates in the crystal: ligand binding to myoglobin

Schlichting, I., & Chu, K. (2000). Trapping intermediates in the crystal: ligand binding to myoglobin. Current Opinion in Structural Biology, 10(6), 744-752. doi:10.1016/S0959-440X(00)00158-5.

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CurrOpinStructBiol_10_2000_744.pdf (Any fulltext), 786KB
 
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 Creators:
Schlichting, Ilme1, Author           
Chu, Kelvin, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Time-resolved crystallography; Laue crystallography; Kinetic crystallography; structural dynamics; photolysis triggering
 Abstract: Crystal structures of the reactive short-lived species that occur in chemical or binding reactions can be determined using X-ray crystallography via time-resolved or kinetic trapping approaches. Recently, various kinetic trapping methods have been used to determine the structure of intermediates in ligand binding to myoglobin.

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Language(s): eng - English
 Dates: 2000-12-062000-12-01
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Current Opinion in Structural Biology
  Other : Curr. Opin. Struct. Biol.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 10 (6) Sequence Number: - Start / End Page: 744 - 752 Identifier: ISSN: 0959-440X
CoNE: https://pure.mpg.de/cone/journals/resource/954925578067