Abstract
Syphilis, caused by the bacterial spirochete Treponema pallidum, remains a prominent sexually transmitted infection worldwide. Despite sequencing of the genome of this obligate human pathogen 15 years ago, the functions of a large number of the gene products of T. pallidum are still unknown, particularly with respect to those of the organism's periplasmic lipoproteins. To better understand their functions, a structural biology approach has been pursued. To this end, the soluble portion of the T. pallidum TP0435 lipoprotein (also known as Tp17) was cloned, hyper-expressed in Escherichia coli and purified to apparent homogeneity. The protein crystals obtained from this preparation diffracted to 2.4 Å resolution and had the symmetry of space group R3. In the hexagonal setting, the unit-cell parameters were a = b = 85.7, c = 85.4 Å.
Original language | English (US) |
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Pages (from-to) | 453-455 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 69 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2013 |
Keywords
- TP0435 (Tp17)
- Treponema pallidum
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics