|
|||||
|
|
Dodecamers derived from the crystal structure were found in the pre-crystallization solution of the transaminase from the thermophilic bacterium Thermobaculum terrenum by small-angle X-ray scattering |
|
| Authors: | Margarita A. Marchenkova Petr V. Konarev Tatiana V. Rakitina Anastasiia S. Boikova Yulia A. Dyakova |
| Affiliation: | 1. Shubnikov Institute of Crystallography of Federal Scientific Research Centre ‘Crystallography and Photonics’ of Russian Academy of Sciences, Moscow, Russian Federation;2. National Research Centre ‘Kurchatov Institute’, Moscow, Russian Federation;3. marchenkova@crys.ras.ru;5. National Research Centre ‘Kurchatov Institute’, Moscow, Russian Federation;6. Shemyakin???Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Hormonal Regulation Proteins, Russian Academy of Sciences, Moscow, Russian Federation |
| Abstract: | AbstractThe 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. Abbreviation SAXS small-angle X-ray scattering Ta transaminase TaTT transaminase from Thermobaculum terrenum PLP pyridoxal-5’-phosphate R-PEA R-(þ)-1-phenylethylamine BCAT branched-chain amino acid aminotransferase DAAT D-aminoacid aminotransferase R-TA R-amine:pyruvate transaminase Communicated by Ramaswamy H. Sarma |
| Keywords: | Small angle X-ray scattering protein crystallization transaminase |