Open AccessCrystallization and preliminary X‐ray diffraction analysis of Salmonella typhi PilS
Author(s) -
Tan Yvonne YihWan,
Mok Henry YuKeung,
Saxena Anand M.,
Balakrishna Asha M.,
Swaminathan Kunchithapadam
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910603661x
Subject(s) - crystallization , crystallography , resolution (logic) , selenium , synchrotron radiation , crystal structure , salmonella typhi , recombinant dna , derivative (finance) , x ray crystallography , materials science , chemistry , diffraction , escherichia coli , physics , optics , biochemistry , organic chemistry , artificial intelligence , computer science , financial economics , economics , gene
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 P 2 1 2 1 2, 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.