Michael Teale

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The crystal structure of the recombinant 19,000 Mr binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 Å resolution. The domain fold is a jelly-roll, composed of two antiparallel β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding(More)
The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 A resolution. The protein crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 57.24, b(More)
One of the most fundamental questions in immunology is how the B lymphocyte immune repertoire develops and diversifies. During ontogeny, there is a temporal appearance of B cells responsive to given antigens during ontogeny (1-8). For example, in the BALB/c strain, B cells responsive to DNP appear first in ontogeny followed by fluorescein,(More)
Receptor activator of NF-kappa B ligand (RANKL) and its receptor activator of NF-kappa B (RANK) play pivotal roles in osteoclast differentiation and function. However, the structural determinants of the RANK that mediate osteoclast formation and function have not been definitively identified. To address this issue, we developed a chimeric receptor approach(More)
Escherichia coli (E. coli) protein 3-methyladenine-DNA glycosylase II (AlkA) functions primarily by removing alkylation damage from duplex and single stranded DNA. A crystal structure of AlkA was refined to 2.0 A resolution. This structure in turn was used to refine an AlkA-hypoxanthine (substrate) complex structure to 2.4 A resolution. The complex(More)
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