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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