Open AccessOverexpression, purification and preliminary crystallographic analysis of human M‐ficolin fibrinogen‐like domain
Author(s) -
Tanio Michikazu,
Kondo Shin,
Sugio Shigetoshi,
Kohno Toshiyuki
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106019786
Subject(s) - ficolin , fibrinogen , domain (mathematical analysis) , crystallography , chemistry , materials science , computational biology , biology , biochemistry , innate immune system , receptor , mathematics , mathematical analysis
Ficolins, which are comprised of a collagen‐like domain and a fibrinogen‐like domain, are a kind of pattern‐recognition molecule for pathogens in the innate immunity system. To investigate the molecular mechanism of the discrimination between self and non‐self by ficolins, human M‐ficolin fibrinogen‐like domain (FD1), which contains the ligand‐binding site, was overexpressed in Pichia pastoris , purified and crystallized using the vapour‐diffusion method at 293 K. The crystals belong to the monoclinic space group P 2 1 , with unit‐cell parameters a = 55.16, b = 117.45, c = 55.19 Å, β = 99.88°, and contain three molecules per asymmetric unit. An X‐ray data set was collected to 1.9 Å resolution using synchrotron radiation at beamline BL24XU at the SPring‐8 facility in Japan.