Crystallization and Preliminary X-ray Diffraction Analysis of Salmonella typhi PilS

Journal Article · Sun Jan 01 00:00:00 EST 2006 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S174430910603661X· OSTI ID:930092

Balakrishna, A; Tan, Y; Mok, H; Saxena, A; Swaminathan, K

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{sub 1}2{sub 1}2, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 {angstrom}. 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 {angstrom} resolution from the selenomethionine-derivative crystal using synchrotron radiation for multiwavelength anomalous dispersion (MAD) phasing.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 930092
• Report Number(s): BNL-80728-2008-JA; TRN: US0806702
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62
• Country of Publication: United States
• Language: English

Related Subjects

43 PARTICLE ACCELERATORS
CRYSTALLIZATION
CRYSTALLOGRAPHY
CRYSTALS
DATA
DISPERSIONS
PROTEINS
RESOLUTION
SALMONELLA
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION
national synchrotron light source