Klenow fragment crystallizing

Beese, L. S., Friedman, J. M., and Steitz, T. A. (1993b). Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry 32, 14095-14101. 

Li, Y., Kong, Y., Korolev, S., and Waksman, G. (1998a). Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleo-side triphosphates. Protein Sci. 7, 1116-1123. 

Section III,A The crystal structure of the NH2-terminal fragment of T4 DNA polymerase was published and its complexes with metal ions and short deoxyoligonucleotides were compared to that of the 3 -5 exonuclease domain of the Klenow fragment (371). 

Figure 32 Time-dependent frequency changes upon the association of avidin-alkaline phosphatase and the biocatalyzed precipitation of (12) in the presence of the oligonu-cleotide/DNA assemblies (a) and (b) correspond to the out of cell interaction of the (SSI-functionalized electrode with (39), 3 x lO" mole-mL and 1 x lO" mole mL, respectively, followed by the reaction of the double-stranded functionalized assemblies with Klenow fragment and biotinylated dCTP, and in cell recording of the frequency changes of the resulting functionalized electrodes upon interaction with avidin-alkaline phosphatase, 100 nmole mL". (c) Out-of-cell interaction of the (38)-functionalized Au-quartz crystal with (40), 3 X 10 mole mL , followed by the reaction of the interface with the Klenow fragment and biotinylated dCTP, and in-cell monitoring of frequency changes upon the interaction of the interface with avidin-alkaline phosphatase, 100 nmole-mL" . (d), (e), and (f) correspond to the time-dependent frequency changes of the respective interfaces formed in (a), (b), and (c) in the presence of (11), 20 mM in 0.1 M Tris-buffer, pH = 7.6, upon the biocatalyzed precipitation of (12).

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