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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization and preliminary X-ray analysis of native and recombinant human bile-salt dependent lipase: strategies for improvement of diffraction quality.

Human bile-salt dependent lipase (BSDL), secreted into both the digestive tract and human milk, is integral to the effective absorption of dietary lipids. In attempts to obtain crystals suitable for high-resolution X-ray crystallographic studies, various forms of the enzyme have been crystallized, including native and desialidated human milk BSDL and both intact recombinant BSDL and a truncated form lacking the heavily glycosylated C-terminal repeat region. Trigonal crystals of native BSDL, with unit-cell parameters a = b = 90.0, c = 156.1 A, were obtained using 15-20%(w/v) PEG 8000 as precipitant. These crystals diffract to 3.5 A along the unique axis, but to only 5-7 A in orthogonal directions. Crystals of recombinant truncated BSDL grown from 15-20%(w/v) PEG 6000 are orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 59.2, b = 90.0, c = 107.7 A, and diffract to 2.6 A resolution. These are suitable for structural analysis by X-ray crystallography.[1]

References

  1. Crystallization and preliminary X-ray analysis of native and recombinant human bile-salt dependent lipase: strategies for improvement of diffraction quality. Kingston, R.L., Baker, H.M., Loomes, K.M., Bläckberg, L., Hernell, O., Baker, E.N. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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