Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 4 (April 2008)

crystallization communications

Acta Cryst. (2008). F64, 284-288 [ doi:10.1107/S1744309108006374 ]

Crystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin-binding protein 2B from Streptococcus pneumoniae

M. Yamada, T. Watanabe, N. Baba, T. Miyara, J. Saito and Y. Takeuchi

Abstract: Penicillin-binding protein (PBP) 2B from Streptococcus pneumoniae catalyzes the cross-linking of peptidoglycan precursors that occurs during bacterial cell-wall biosynthesis. A selenomethionyl (SeMet) substituted PBP 2B transpeptidase domain was isolated from a limited proteolysis digest of a soluble form of recombinant PBP 2B and then crystallized. The crystals belonged to space group P4₃2₁2, with unit-cell parameters a = b = 86.39, c = 143.27 Å. Diffraction data were collected to 2.4 Å resolution using the BL32B2 beamline at SPring-8. The asymmetric unit contains one protein molecule and 63.7% solvent.

Keywords: antibiotics; -lactams; peptidoglycan synthesis; cell wall.