Open AccessCrystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis
Author(s) -
Khan Abdul Hamid,
Mohamed Omar Youssef Mohamed,
Kakar Mohammad Azam,
Bangulzai Nasrullah
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113012554
Subject(s) - recombinant dna , crystallization , lyase , bacteria , escherichia coli , chemistry , crystallography , enzyme , materials science , biochemistry , biology , gene , organic chemistry , genetics
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 P 222 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.