Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain.
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 P2(1), with unit-cell parameters a = 55.16, b = 117.45, c = 55.19 angstroms, beta = 99.88 degrees, and contain three molecules per asymmetric unit. An X-ray data set was collected to 1.9 angstroms resolution using synchrotron radiation at beamline BL24XU at the SPring-8 facility in Japan.
Tanio
Michikazu
M
Mitsubishi Kagaku Institute of Life Sciences (MITILS), Minamiooya 11, Machida, Tokyo 194-8511, Japan.
Kondo
Shin
S
Sugio
Shigetoshi
S
Kohno
Toshiyuki
T
D018360:Crystallography, X-Ray; D005340:Fibrinogen; D006801:Humans; D007113:Immunity, Innate; D037102:Lectins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D008958:Models, Molecular; D010843:Pichia / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D017356:Synchrotrons; D000097604:Ficolins
D005340:Fibrinogen; D037102:Lectins; D011994:Recombinant Proteins; D000097604:Ficolins