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- W2964759937 abstract "The pre-crystallization solution of the transaminase from Thermobaculum terrenum (TaTT) has been studied by small-angle X-ray scattering (SAXS). Regular changes in the oligomeric composition of the protein were observed after the addition of the precipitant. Comparison of the observed oligomers with the crystal structure of TaTT (PDB ID 6GKR) shows that dodecamers may act as building blocks in the growth of transaminase single crystals. Correlating of these results to the similar X-ray studies of other proteins suggests that SAXS may be a valuable tool for searching optimum crystallization conditions. AbbreviationSAXSsmall-angle X-ray scatteringTatransaminaseTaTTtransaminase from Thermobaculum terrenum PLPpyridoxal-5’-phosphateR-PEAR-(þ)-1-phenylethylamineBCATbranched-chain amino acid aminotransferaseDAATD-aminoacid aminotransferaseR-TAR-amine:pyruvate transaminase Communicated by Ramaswamy H. Sarma" @default.
- W2964759937 created "2019-08-13" @default.
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- W2964759937 date "2019-08-08" @default.
- W2964759937 modified "2023-10-16" @default.
- W2964759937 title "Dodecamers derived from the crystal structure were found in the pre-crystallization solution of the transaminase from the thermophilic bacterium <i>Thermobaculum terrenum</i> by small-angle X-ray scattering" @default.
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- W2964759937 doi "https://doi.org/10.1080/07391102.2019.1649195" @default.
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