Overexpression, purification and crystallization of a choline‐binding protein CbpI from Streptococcus pneumoniae
The choline‐binding protein CbpI from Streptococcus pneumoniae is a 23.4 kDa protein with no known function. The protein has been successfully purified initially using Ni–NTA chromatography and to homogeneity using Q‐Sepharose ion‐exchange resin as an affinity column. CbpI was crystallized using PEG 3350 as a precipitant and X‐ray crystallographic analysis showed that the crystals belonged to the tetragonal space group P4, with unit‐cell parameters a = b = 83.31, c = 80.29 Å, α = β = γ = 90°. The crystal contains two molecules in the asymmetric unit with a solvent content of 55.7% (V M = 2.77 Å3 Da−1) and shows a diffraction limit of 3.5 Å.
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