Overexpression, purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain

Journal Article · Sat Jul 01 04:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106019786· OSTI ID:22360197

Tanio, Michikazu ^[1]; Kondo, Shin; Sugio, Shigetoshi ^[2]; Kohno, Toshiyuki ^[1]

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1. Mitsubishi Kagaku Institute of Life Sciences (MITILS), Minamiooya 11, Machida, Tokyo 194-8511 (Japan)
2. ZOEGENE Corporation, 1000 Kamoshida, Aoba, Yokohama 227-8502 (Japan)

Human M-ficolin fibrinogen-like domain has been overexpressed in P. pastoris, purified and crystallized. Diffraction data have been collected to 1.9 Å. 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{sub 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.

• OSTI ID: 22360197
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
COLLAGEN
CRYSTALS
DIFFRACTION
DIFFUSION
LIGANDS
MOLECULES
PATTERN RECOGNITION
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION