Crystallization and X-ray analysis of Borrelia burgdorferi β-barrel assembly machinery A.

Mitochondria, chloroplasts and several species of bacteria have outer membrane proteins (OMPs) that perform many essential biological functions. The β-barrel assembly machinery (BAM) complex is one of the OMPs of Borrelia burgdorferi, the pathogenic spirochete that causes Lyme disease, and its BamA component (BbBamA) includes a C-terminal β-barrel domain and five N-terminal periplasmic polypeptide-transport-associated (POTRA) domains, which together perform a central transport function. In the current work, the production, crystallization and X-ray analysis of the three N-terminal POTRA domains of BbBamA (BbBamA-POTRA P1-P3; residues 30-273) were carried out.

Crystal structure of the Měnglà virus VP30 C-terminal domain.

The family Filoviridae contains many important human viruses, including Marburg virus (MARV) and Ebola virus (EBOV). Měnglà virus (MLAV), a newly discovered filovirus, is considered a potential human pathogen. The VP30 C-terminal domain (CTD) of these filoviruses plays an essential role in virion assembly.