In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 72, No. 12 ( 2016-12-01), p. 877-884
Abstract:
Viral proteases are proteolytic enzymes that orchestrate the assembly of viral components during the viral life cycle and proliferation. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis are presented of protease 3C, the main protease of an emerging enterovirus, coxsackievirus B3, that is responsible for many cases of viral myocarditis. Polycrystalline protein precipitates suitable for X-ray powder diffraction (XRPD) measurements were produced in the presence of 22–28%( w / v ) PEG 4000, 0.1 M Tris–HCl, 0.2 M MgCl 2 in a pH range from 7.0 to 8.5. A polymorph of monoclinic symmetry (space group C 2, unit-cell parameters a = 77.9, b = 65.7, c = 40.6 Å, β = 115.9°) was identified via XRPD. These results are the first step towards the complete structural determination of the molecule via XRPD and a parallel demonstration of the accuracy of the method.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X16018513
DOI:
10.1107/S2053230X16018513/wd5269sup1.pdf
DOI:
10.1107/S2053230X16018513/wd5269sup2.txt
DOI:
10.1107/S2053230X16018513/wd5269sup3.txt
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2016
detail.hit.zdb_id:
2175956-X
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