Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS

Please use this identifier to cite or link to this item: https://doi.org/10.1107/S174430910603661X

Title:	Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS
Authors:	Tan, Y.Y.-W. Mok, H.Y.-K. Saxena, A.M. Balakrishna, A.M. Swaminathan, K.
Keywords:	PilS Salmonella typhi Type IV pilin
Issue Date:	Oct-2006
Citation:	Tan, Y.Y.-W., Mok, H.Y.-K., Saxena, A.M., Balakrishna, A.M., Swaminathan, K. (2006-10). Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 62 (10) : 1024-1026. ScholarBank@NUS Repository. https://doi.org/10.1107/S174430910603661X
Abstract:	The structure determination of PilS, a type IV pilin, by X-ray crystallography is reported. The recombinant protein from Salmonella typhi was overexpressed, purified and crystallized. The crystals belong to space group P21212, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 Å. The selenomethionine derivative of the PilS protein was overexpressed, purified and crystallized in the same space group. Data sets have been collected to 2.1 Å resolution from the selenomethionine-derivative crystal using synchrotron radiation for multiwavelength anomalous dispersion (MAD) phasing. © International Union of Crystallography, 2006.
Source Title:	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
URI:	http://scholarbank.nus.edu.sg/handle/10635/100376
ISSN:	17443091
DOI:	10.1107/S174430910603661X
Appears in Collections:	Staff Publications

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