Crystallization of a 79kDa fragment of the hook protein FlgE from Campylobacter jejuni
A 79kDa fragment of the bacterial flagellar hook protein FlgE from Campylobacter jejuni was cloned, overexpressed, purified and crystallized. Two different crystal forms were obtained. Synchrotron X-ray diffraction data showed that the first crystal form, which diffracted to 4.9Aa resolution, belong...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-12, Vol.67 (12), p.1653-1657 |
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Sprache: | eng |
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Zusammenfassung: | A 79kDa fragment of the bacterial flagellar hook protein FlgE from Campylobacter jejuni was cloned, overexpressed, purified and crystallized. Two different crystal forms were obtained. Synchrotron X-ray diffraction data showed that the first crystal form, which diffracted to 4.9Aa resolution, belonged to the tetragonal crystal system, with space group I4122 and unit-cell parameters a = b = 186.2, c = 386.6Aa, alpha = beta = gamma = 90 degree . The second crystal form diffracted to 2.5Aa resolution and belonged to the monoclinic crystal system, with space group P21 and unit-cell parameters a = 75.7, b = 173.8, c = 150.8Aa, alpha = gamma = 90, beta = 106.5 degree . SeMet protein was also overexpressed, purified and crystallized, and a 2.6Aa resolution MAD data set was collected. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309111043272 |