Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement-Reference-Cited by-同舟云学术

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Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement

Published:2009-01-09 Issue:3 Volume:106 Page:713-718
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:PNAS

Author:

Blum Marc-Michael,Mustyakimov Marat,Rüterjans Heinz,Kehe Kai,Schoenborn Benno P.,Langan Paul,Chen Julian C.-H.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference37 articles.

1. Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin;Kossiakoff;Biochemistry,1981

2. Structure of ribonuclease A: results of joint neutron and x-ray refinement at 2.0-.ANG. resolution

3. Locating active-site hydrogen atoms in D-xylose isomerase: Time-of-flight neutron diffraction

4. Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate

5. A neutron Laue diffraction study of endothiapepsin: Implications for the aspartic proteinase mechanism;Coates;Biochemistry,2001

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