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- W2022098805 abstract "Rapana thomasiana hemocyanin is a representative of molluscan (gastropodan) dioxygen-transporting proteins. The cylindrical hemocyanin aggregates are composed of two structural subunits, RHSS1 and RHSS2. The 420 kDa subunit RHSS2 contains eight 50–55 kDa functional units. Each unit has a single dioxygen-binding dinuclear copper-containing active site. Molluscan hemocyanin functional units can be subdivided into “internal units”, forming the so-called “arch” inside the hemocyanin cylinders, and “external” units, building the cylinder wall of the aggregates. The “external” oxygenated functional unit RtH2-e of the Rapana hemocyanin subunit RHSS2 was isolated and crystallized in two crystal forms. Type I crystals are small but X-ray suitable and show bipyramidal morphology. Preliminary data were collected to 3.3 Å at 120 K using synchrotron radiation. The space group is assigned to be the tetragonal P41212 or its enantiomer with unit cell dimensions a=b=105.5 Å and c=375.0 Å. Type II crystals grow in thin plates and diffract to about 3.0 Å. However, they are always twinned and cannot be utilized for data collection and structure analysis." @default.
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- W2022098805 date "2001-11-01" @default.
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- W2022098805 title "Crystallization, preliminary X-ray analysis and amino acid sequence studies of an “external” functional unit from the Rapana thomasiana grosse (mollusc, gastropod) hemocyanin" @default.
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- W2022098805 doi "https://doi.org/10.1016/s0022-0248(01)01055-7" @default.
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