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  • 1
    Electronic Resource
    Electronic Resource
    Expression, purification, crystallization and preliminary X-ray analysis of the cathelicidin motif of the protegrin-3 precursor (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1677-1679 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Numerous precursors of antibacterial peptides with unrelated sequences share a similar prosequence which belongs to the cathelicidin family of proteins. The three-dimensional structure of this cathelicidin motif, which contains two disulfide bonds, has not yet been reported. The cathelicidin motif (ProS) of the protegrin-3 precursor was overexpressed in Escherichia coli as a His-tagged protein. The His6 tag was removed by thrombin cleavage. ProS was purified to homogeneity and single crystals were obtained by the hanging-drop vapour-diffusion method at pH 3–4. Preliminary X-ray diffraction analysis indicated that these crystals belong to the hexagonal space group P6122 or P6522, with unit-cell parameters a = b = 51.42, c = 134.25 Å. These crystals diffracted beyond 2.75 Å (1.9 Å at ESRF) and contain one molecule per asymmetric unit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012598
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization of previously desalted lysozyme in the presence of sulfate ions (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 366-369 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Lysozyme, which is known to crystallize readily in the presence of many salts, has never been crystallized by salting out with ammonium sulfate. In the present study, lysozyme was first completely desalted by treatment with strong cation- (H+ form) and anion- (OH− form) exchange resins. This leads to a protein solution with only H+ and OH− as counterions, corresponding to its isoionic point. Addition of 2.5–3 molar equivalents of H2SO4 to isoionic lysozyme decreases the pH value to 9–8 and allows crystallization to take place. The space group was found to be P43212, similar to the classical lysozyme crystals grown in the presence of NaCl at pH 4.5, with unit-cell dimensions a = b = 78.9, c = 38.5 Å. Tentative explanation of the sulfate/lysozyme interaction was addressed by mass spectrometry, and shows non-covalent binding of the ions on the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994001320
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  • 3
    Electronic Resource
    Electronic Resource
    Production of crystals of human aldose reductase with very high resolution diffraction (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 721-723 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: As the action of human aldose reductase (hAR) is thought to be linked to the pathogenesis of diabetic complications, much effort has been directed towards the analysis of the catalytic mechanism and the development of specific inhibitors. Here, the crystallization of recombinant hAR with its cofactor NADP+ at 277 K in the presence of the precipitating agent PEG 6000 is reported. The crystals diffract to high resolution (1.1 Å) and belong to the P21 space group with unit-cell parameters a = 49.97, b = 67.14, c = 48.02 Å, β = 92.2° with one molecule per asymmetric unit. Seleno-substituted hAR crystals were also produced and diffract to 1.7 Å on a conventional X-ray source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998013365
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of crystal content by ESI–MS and MALDI–MS (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1583-1590 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A general approach based on mass spectrometry is described for the rapid identification of the content of macromolecular crystals. The experimental procedure was established using lysozyme crystals and then successfully applied to various systems containing specifically bound molecules not easily detectable by other classical techniques. This procedure can be carried out on crystals containing macromolecules of a different nature, such as proteins, nucleic acids and small organic molecules and their non-covalent complexes, grown under various crystallization conditions including PEGs and salts. It can be applied very early on in the crystallization process – as soon as the crystals can be handled. It allows the biologist to control precisely the sequence integrity and homogeneity of the crystallized proteins (in particular at the C-terminus) as well as to verify whether the protein has crystallized with all its expected partners or ligands (nucleic acid molecules, cofactor or small organic molecules).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900010271
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