Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Mia L. Raves"'
Autor:
Jurgen F. Doreleijers, Mia L. Raves, Keith S. Wilson, Robert Kaptein, Constantin E. Vorgias, Hans Vis
Publikováno v:
Journal of Biomolecular NMR. 21:235-248
Joint refinement, i.e., the simultaneous refinement of a structure against both nuclear magnetic resonance (NMR) spectroscopic and X-ray crystallographic data, was performed on the HU protein from Bacillus stearothermophilus (HUBst). The procedure wa
Publikováno v:
Proteins: Structure, Function, and Genetics. 37:404-416
A statistical analysis is reported of 1,200 of the 1,404 nuclear magnetic resonance (NMR)-derived protein and nucleic acid structures deposited in the Protein Data Bank (PDB) before 1999. Excluded from this analysis were the entries not yet fully val
Publikováno v:
Journal of Biomolecular NMR. 14:123-132
The completeness of experimentally observed NOE restraints of a set of 97 NMR protein structures deposited in the PDB has been assessed. Completeness is defined as the ratio of the number of experimentally observed NOEs and the number of 'expected NO
Publikováno v:
Journal of Synchrotron Radiation. 6:19-28
The potential of using polychromatic synchrotron radiation for ab initio structure determination of low-molecular-weight compounds is investigated. Three different organic compounds were studied. For each of the structures the cell volume was determi
Autor:
Joan R. Kanter, Joel L. Sussman, Palmer Taylor, Pascale Marchot, Raimond B. G. Ravelli, Shelley Camp, Mia L. Raves, Daniel C. Vellom, Yves Bourne
Publikováno v:
Protein Science. 5:672-679
A soluble, monomeric form of acetylcholinesterase from mouse (mAChE), truncated at its carboxyl-terminal end, was generated from a cDNA encoding the glycophospholipid-linked form of the mouse enzyme by insertion of an early stop codon at position 549
Publikováno v:
Biochemical Society Transactions. 22:745-749
Publikováno v:
Journal of Molecular Structure. 271:109-118
Crystallisation of the “proton sponge” 1,8-bis(dimethylamino)naphthalene (DMAN) in the presence of hemimellitic acid (1,2,3-benzenetricarboxylic acid, BTA) resulted in the salt [DMANH]+·[BTA]−· 1 2 H2O. The structure analysis was performed at
Autor:
Joel L. Sussman, Jan Kroon, Raimond B. G. Ravelli, Dominique Bourgeois, Mia L. Raves, Michel Roth, Israel Silman, Zhong Ren
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 54(Pt 6 Pt 2)
Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to,
Publikováno v:
Advances in Behavioral Biology ISBN: 9781461374350
Acetylcholinesterase (AChE) terminates synaptic transmission at cholinergic synapses by rapid hydrolysis of acetylcholine (ACh) (Quinn, 1987). Anticholinesterase agents are used in the treatment of various disorders (Taylor, 1990), and have been prop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::980067f2c2b4dd3656d8cce93a189e84
https://doi.org/10.1007/978-1-4615-5337-3_75
https://doi.org/10.1007/978-1-4615-5337-3_75
Autor:
Michal Harel, Raimond B. G. Ravelli, Harry M. Greenblatt, Mia L. Raves, Joel L. Sussman, Israel Silman, Gitay Kryger, Anne Nicolas, Jan Kroon
Publikováno v:
Structure and Function of Cholinesterases and Related Proteins ISBN: 9781489915429
Proteins often form crystals of different shapes and sizes, depending on crystallisation conditions such as pH, temperature, concentration and nature of precipitant, and the presence or absence of additives. In addition to the macroscopic variety and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::66bacf3d64ea4aef69aed6022ab46e0b
https://doi.org/10.1007/978-1-4899-1540-5_104
https://doi.org/10.1007/978-1-4899-1540-5_104