title: Crystallization of recombinant Haemophilus influenzae e (P4) acid phosphatase.
abstract: Haemophilus influenzae infects the upper respiratory tract of humans and can cause infections of the middle ear, sinuses and bronchi. The virulence of the pathogen is thought to involve a group of surface-localized macromolecular components that mediate interactions at the host-pathogen interface. One of these components is lipoprotein e (P4), which is a class C acid phosphatase and a potential vaccine candidate for nontypeable H. influenzae infections. This paper reports the crystallization of recombinant e (P4) and the acquisition of a 1.7 angstroms resolution native X-ray diffraction data set. The space group is P4(2)2(1)2, with unit-cell parameters a = 65.6, c = 101.4 angstroms, one protein molecule per asymmetric unit and 37% solvent content. This is the first report of the crystallization of a class C acid phosphatase.
authors: Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211, USA.
authors: Zhonghui
authors: Z
authors: Ou
authors: Richard L
authors: RL
authors: Felts
authors: Thomas J
authors: TJ
authors: Reilly
authors: Jay C
authors: JC
authors: Nix
authors: John J
authors: JJ
authors: Tanner