Zobrazeno 1 - 8
of 8
pro vyhledávání: '"R. F. Tilton"'
Publikováno v:
Journal of Applied Crystallography. 26:309-319
Two crystals of monoclinic hen egg-white lysozyme were irradiated in a monochromatic synchrotron X-ray beam (λ = 1.488 A), the first as a rapidly frozen crystal mounted at the end of a glass fiber at low temperature (120 K) and the second mounted in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48032a4e902b3c86a7a4cc1ce211a55c
https://doi.org/10.1107/s0021889892010070
https://doi.org/10.1107/s0021889892010070
Publikováno v:
Journal of the American Chemical Society. 114:4447-4452
The free energy perturbation method has been employed to determine the binding free energy contributions of different groups of two classes of HIV-1 proteinase inhibitors: (1) a hydroxyethylene isostere inhibitor, Ala-Ala-Phe[CH(OH)CH 2 ]Gly-Val-Val-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4cb18b2a69d32b431411dd6c15ff22d5
https://doi.org/10.1021/ja00038a001
https://doi.org/10.1021/ja00038a001
Publikováno v:
Journal of molecular biology. 235(1)
The average structural and dynamic properties of tetragonal hen egg-white lysozyme have been compared, in structures refined at 1.9 A resolution, using data collected at 100 K and 298 K. The molecule expands by 1.8% over this temperature range with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::caaa9af1e843f506453e8b598bb8c82e
https://pubmed.ncbi.nlm.nih.gov/8289250
https://pubmed.ncbi.nlm.nih.gov/8289250
Publikováno v:
The Journal of Physical Chemistry. 89:289-294
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1607eb28f07d316176b5420a43749a7a
https://doi.org/10.1021/j100248a023
https://doi.org/10.1021/j100248a023
Autor:
R. F. Tilton
Publikováno v:
Journal of Applied Crystallography. 21:4-10
A fixture is described for collecting X-ray diffraction data from biomolecule crystals under gas pressures up to 300 atm (30 MPa). The fixture is completely portable and can be used on conventional diffractometers. Normal procedures for crystal mount
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6503a7890fc861a4bab903a6714c59fb
https://doi.org/10.1107/s0021889887008173
https://doi.org/10.1107/s0021889887008173
Autor:
H, Frauenfelder, H, Hartmann, M, Karplus, I D, Kuntz, J, Kuriyan, F, Parak, G A, Petsko, D, Ringe, R F, Tilton, M L, Connolly
Publikováno v:
Biochemistry. 26(1)
The thermal expansion of a protein, metmyoglobin, was investigated by analysis of the refined X-ray crystal structures at 80 and 255-300 K. On heating from 80 to 300 K, the volume occupied by myoglobin increases by approximately 3%. The linear therma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c115fa02a7463f90dd2d472a7b2cb15
https://pubmed.ncbi.nlm.nih.gov/3828301
https://pubmed.ncbi.nlm.nih.gov/3828301
Publikováno v:
Chemischer Informationsdienst. 16
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::10f127d7111db7a3e451acff97656249
https://doi.org/10.1002/chin.198523051
https://doi.org/10.1002/chin.198523051
Autor:
R. F. Tilton, J. C. Dewan
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 43:C8-C9
X-ray data have been collected from crystals of bovine pancreatic ribonuclease A at temperatures of 220K and below, by use of a nitrogen-gas cold stream and a computer-controlled diffractometer. One data set, collected from a crystal mounted in the t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4290eae0374dd033683a191c141fb2e5
https://doi.org/10.1107/s0108767387085313
https://doi.org/10.1107/s0108767387085313