Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea
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Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
|Journal||Acta Crystallographica. Section D: Biological Crystallography|
|Issue number||Pt 2|
|Number of pages||3|
|Publication status||Published - Feb 2000|
- Bacterial Proteins, Circular Dichroism, Crystallization, Crystallography, X-Ray, Escherichia coli, Glucosyltransferases, Neisseria, Recombinant Proteins