Výsledky vyhledávání - "Geoffrey C. Ford"

An application of the molecular replacement technique in direct space to a known protein structure

Autor: Geoffrey C. Ford, Patrick Argos, Michael G. Rossmann

Publikováno v: Acta Crystallographica Section A. 31:499-506

The molecular replacement technique in real space (successive cycles of electron density calculations, averaging among non-crystallographically equivalent subunits, and structure factor calculations based upon the improved averaged density) was appli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ca1853b37d75d510d882c3e4aeff65c7
https://doi.org/10.1107/s0567739475001076

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Crystallization and preliminary X-ray crystallographic data of the bifunctional enzyme phosphoribosyl-anthranilate isomerase-indole-3-glycerol-phosphate synthase fromEscherichia coli

Autor: M.G. Grütter, E. Wilson, J.D.G. Smit, Johan N. Jansonius, Geoffrey C. Ford, J.L. White, Kasper Kirschner, Christina Thaller

Publikováno v: FEBS Letters. 148:87-90

Phosphoribosyl-anthranilate isomerase: indole—3-glycerol-phosphate-synthase, a monomeric bifunctional enzyme of Mr = 49 500 from Escherichia coli, catalyses 2 sequential reactions in the synthesis of tryptophan from chorismate. Its amino acid seque

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10ecb561ae7687bd4e0ce7fd6ce519da
https://doi.org/10.1016/0014-5793(82)81248-9

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Three-dimensional structure of mitochondrial aspartate aminotransferase and some functional derivatives: implications for its mode of action

Autor: J. F. Kirsch, Johan N. Jansonius, M. G. Vincent, Geoffrey C. Ford, D. Picot, Gregor Eichele, Heinz Gehring, Christina Thaller, Philipp Christen

Publikováno v: Biochemical Society Transactions. 12:424-427

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f2a478762b919cf9a354a1df1b26c57
https://doi.org/10.1042/bst0120424

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Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme Complexes

Autor: Richard W. Schevitz, Ira E. Smiley, Marvin L. Hackert, M.J. Adams, Alexander McPherson, Geoffrey C. Ford, Paul J. Lentz, Michael G. Rossmann, Manfred Buehner

Publikováno v: Cold Spring Harbor Symposia on Quantitative Biology. 36:179-191

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c780d4dccbbc5422d69e05d560aaf9a
https://doi.org/10.1101/sqb.1972.036.01.025

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Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase

Autor: Margaret J. Adams, Michael G. Rossmann, Anders Liljas, Geoffrey C. Ford

Publikováno v: Biochemical and Biophysical Research Communications. 53:46-51

Atomic co-ordinates for one subunit of LDH are given in A with respect to a Cartesian co-ordinate system corresponding to the molecular two-fold axes.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff5d62b0cde835a0b9cfd4b3ce962e88
https://doi.org/10.1016/0006-291x(73)91398-3

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D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance

Autor: Dino Moras, Manfred Buehner, Michael G. Rossmann, Geoffrey C. Ford, Kenneth W. Olsen

Publikováno v: Proceedings of the National Academy of Sciences. 70:3052-3054

A 3.0-Å resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2892e2a879c5a5be116695df1a55a139
https://doi.org/10.1073/pnas.70.11.3052

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Structure determination of crystalline lobster D-glyceraldehyde-3-phosphate dehydrogenase

Autor: Dino Moras, Geoffrey C. Ford, Manfred Buehner, Michael G. Rossmann, Kenneth W. Olsen

Publikováno v: Journal of molecular biology. 82(4)

Single crystal X-ray data were collected on film for the holoenzyme of lobster d -glyceraldehyde-3-phosphate dehydrogenase to 3·0 A resolution. Films of potassium tetraiodomercurate, K 2 HgI 4 , comprising a complete low resolution set, with some ad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3df92a4dc82e43363ef7d6356026e997
https://pubmed.ncbi.nlm.nih.gov/4817797

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