Author: Myllykoski, Matti; Kursula, Petri
Title: Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase Document date: 2017_1_31
ID: 0a3okta0_49
Snippet: Small-angle X-ray scattering SAXS data were collected in batch mode on the EMBL/DESY synchrotron beamline P12 [52] , using standard procedures [53] . In addition to LigT alone, yeast tRNA (Sigma) and a 1:1 molar mixture of LigT and tRNA were analyzed. Data were processed with the ATSAS package [54] . Distance distribution functions were analyzed using GNOM [55] . For modelling LigT alone, GASBOR [56] was used. For modelling the protein-RNA comple.....
Document: Small-angle X-ray scattering SAXS data were collected in batch mode on the EMBL/DESY synchrotron beamline P12 [52] , using standard procedures [53] . In addition to LigT alone, yeast tRNA (Sigma) and a 1:1 molar mixture of LigT and tRNA were analyzed. Data were processed with the ATSAS package [54] . Distance distribution functions were analyzed using GNOM [55] . For modelling LigT alone, GASBOR [56] was used. For modelling the protein-RNA complex, we used the program MONSA [57] with the protein and RNA in different phases. The tRNA alone was modelled using DAMMIN [57] . Molecular weight was estimated through a comparison of the forward scattering intensity of the sample to that of a fresh sample of monomeric bovine serum albumin.
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