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|Title:||Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS||Authors:||Tan, Y.Y.-W.
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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