title: Crystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis.
abstract: Hyaluronate lyase is an important surface enzyme of many streptococcal species. The enzyme degrades several biologically important connective tissue components, which facilitates the spreading of the bacteria throughout the host tissues and presumably provides energy and a carbon source for bacterial cells. Recombinant hyaluronate lyase was expressed in Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P222(1), with unit-cell parameters a = 58.08, b = 101.32, c = 103.47 Å and one molecule in the asymmetric unit. Diffraction data were collected to 2.50 Å resolution.
authors.affiliation: Department of Microbiology, Lasbela University of Agriculture, Water and Marine Sciences, Uthal, Pakistan. hamidnut@yahoo.com
authors.forename: Abdul Hamid
authors.initials: AH
authors.lastname: Khan
authors.forename: Youssef Mohamed
authors.initials: YM
authors.lastname: Mohamed Omar
authors.forename: Mohammad Azam
authors.initials: MA
authors.lastname: Kakar
authors.forename: Nasrullah
authors.initials: N
authors.lastname: Bangulzai
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017011:Streptococcus suis / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D011133:Polysaccharide-Lyases; C100002:hyaluronate lyase
keywords: Streptococcus suis; hyaluronate lyase