Abstract
A fully active 83-kDa truncated form of recombinant hyaluronate lyase fromStreptococcus pneumoniaewas crystallized by the hanging drop vapor diffusion method using ammonium sulfate as a precipitating agent. Crystals grew at room temperature using a variety of buffers with pH around 6. The crystals diffract X-rays beyond 2.0 Å resolution using Cu Kα radiation and a rotating-anode X-ray source. They belong to the orthorhombic space group P212121with unit cell dimensions,a= 84.2,b= 104.2,c= 104.6 Å, and α = β = γ = 90.0°. TheVMvalue of 2.9 Å3/Da is consistent with only one molecule of the enzyme in the asymmetric unit and the solvent content of 57%. Diffraction data 94.7% complete to 2.0 Å resolution withRsymof 5.4% were collected from one native crystal at room temperature. The search for heavy-atom derivatives to solve the structure is in progress.
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