title: Purification, crystallization and preliminary X-ray analysis of TP0435 (Tp17) from the syphilis spirochete Treponema pallidum.
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.
authors.affiliation: Department of Biophysics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA. chad.brautigam@utsouthwestern.edu
authors.forename: Chad A
authors.initials: CA
authors.lastname: Brautigam
authors.forename: Ranjit K
authors.initials: RK
authors.lastname: Deka
authors.forename: Michael V
authors.initials: MV
authors.lastname: Norgard
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D008074:Lipoproteins / Q000737:chemistry* / Q000302:isolation & purification; D014210:Treponema pallidum / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D008074:Lipoproteins
keywords: TP0435 (Tp17); Treponema pallidum
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