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Updated: Jun 23, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Expression, purification, crystallization and preliminary crystallographic analysis of laminin-binding protein (Lmb)
Preethi Ragunathan1, Barbara Spellerberg, Karthe Ponnuraj
1Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Chennai, India. pkarthe@hotmail.com
Abstract:
Laminin-binding protein (Lmb), a surface-exposed lipoprotein from Streptococcus agalactiae (group B streptococcus), mediates attachment to human laminin and plays a crucial role in the adhesion/invasion of eukaryotic host cells. However, the structural basis of laminin binding still remains unclear. In the context of detailed structural analysis, the lmb gene has been cloned, expressed in Escherichia coli, purified and crystallized. The crystals diffracted to a resolution of 2.5 A and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 56.63, b = 70.60, c = 75.37 A, beta = 96.77 degrees .

