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In this study, we examined the interaction with model DNA substrates of a Rap1DBD construct that comprises residues 358 601 (DBD) observed in the most recent crystal structure.
However, the most recent crystal structure of SeCobAWT with Co II Cbl and MgATP bound shows instead that a nearby phenylalanine (F91) residue is positioned on the face of the corrin ring where the DMB group is usually found.
The DNA-binding domain (DBD) of yeast Rap1 is centrally positioned within the full-length protein sequence, spanning residues 358 601 based on electron density provided from the most recent crystal structure of the DBD DNA complex.
These results are in agreement with the bond distances and angles of the enzyme-bound 5c and 4c Co II Cbl species derived from the most recent crystal structure of SeCobAWT (Table 1).
The most recent crystal structure of the DBD bound to a TeloA sequence shows that the ∼30 amino acids in the C-terminal region of the DBD (wrapping loop) fold back onto the N-terminal Myb-like domain to form a closed complex on DNA.
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We generated a construct of the DNA-binding domain of S. cerevisiae Rap1 that comprises residues 358 601 (DBD), as observed in the most recent X-ray crystal structure in complex with DNA.
With a £300m fortune, John – who is on a 300-date retirement tour – can afford to shop in luxury stores, but he professes to be a John Lewis regular, with some Dartington crystal glasses his most recent purchase.
Wilczek opened the scientific part of the symposium by presenting one of his own most recent theoretical concepts, known as time crystals.
It is also known for partly inspiring the crystal skull in the most recent Indiana Jones film, according to his keeper, JoAnn Parks.
This article provides an overview of the most recent advances regarding the growth of membrane protein crystals and how to best assess crystal quality-diffraction in a high-throughput fashion using synchrotron radiation.
The most recent results obtained in particle beams with realistic crystal prototypes are also presented.
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