Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS.
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 P2(1)2(1)2, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 A. 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 A resolution from the selenomethionine-derivative crystal using synchrotron radiation for multiwavelength anomalous dispersion (MAD) phasing.
Balakrishna
Asha M
AM
Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
Tan
Yvonne Yih-Wan
YY
Mok
Henry Yu-Keung
HY
Saxena
Anand M
AM
Swaminathan
Kunchithapadam
K
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D018360:Crystallography, X-Ray; D036781:Fimbriae Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012485:Salmonella typhi / Q000737:chemistry*; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D017356:Synchrotrons; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D036781:Fimbriae Proteins; D012645:Selenomethionine