Expression, purification, crystallization and preliminary crystallographic analysis of laminin-binding protein (Lmb) from Streptococcus agalactiae.
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 .
Ragunathan
Preethi
P
Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Chennai, India. pkarthe@hotmail.com
Spellerberg
Barbara
B
Ponnuraj
Karthe
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D017474:Receptors, Laminin / Q000032:analysis* / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013292:Streptococcus agalactiae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D017474:Receptors, Laminin