Open AccessCrystallization of recombinant Haemophilus influenzae e (P4) acid phosphatase
Author(s) -
Ou Zhonghui,
Felts Richard L.,
Reilly Thomas J.,
Nix Jay C.,
Tanner John J.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106012358
Subject(s) - crystallization , haemophilus influenzae , recombinant dna , pathogen , acid phosphatase , phosphatase , microbiology and biotechnology , human pathogen , virulence , biology , bacteria , chemistry , biochemistry , enzyme , gene , genetics , organic chemistry , antibiotics
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 Å resolution native X‐ray diffraction data set. The space group is P 4 2 2 1 2, with unit‐cell parameters a = 65.6, c = 101.4 Å, one protein molecule per asymmetric unit and 37% solvent content. This is the first report of the crystallization of a class C acid phosphatase.