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- W2040766036 abstract "Crystals have been obtained of the recombinant human adenovirus serotype 2 proteinase (AVP) in a complex with its 11-amino-acid cofactor pVIc. AVP–pVIc complexes were formed by the incubation of AVP with a 1.2-fold molar excess of pVIc prior to the crystallization trials. Diffraction-quality crystals were obtained at 18°C by the vapor-diffusion method with 5.6 mg/ml AVP–pVIc in 1.4Msodium acetate and 0.1MHepes, pH 7.5. Diffraction data (99% complete to 2.6 Å resolution withRmergeof 0.077) were collected from native crystals at room temperature at beamline X12-C at the National Synchrotron Light Source. The crystals belong to space group P61with unit cell dimensionsa=b= 114.2 Å,c= 50.1 Å; α = β = 90°, γ = 120°. The unit cell dimensions and likely mass of the molecular species in the crystals were consistent with there being one 25 000-Da complex (1:1) per asymmetric unit. Additionally, one heavy-atom derivative, obtained by the soaking of preformed crystals, was isomorphous to the native crystal. Diffraction data obtained on these crystals were 95% complete to 3.0 Å resolution with anRmergeof 0.076. Difference-Patterson analysis indicates three heavy atom sites in the derivative asymmetric unit." @default.
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- W2040766036 date "1996-07-01" @default.
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- W2040766036 title "Preparation and Crystallization of a Complex between Human Adenovirus Serotype 2 Proteinase and Its 11-Amino-Acid Cofactor pVIc" @default.
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- W2040766036 doi "https://doi.org/10.1006/jsbi.1996.0072" @default.
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