Send to

Choose Destination
Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):388-92. doi: 10.1107/S2053230X1500360X. Epub 2015 Mar 20.

Crystallization and preliminary X-ray crystallographic analysis of the sclerostin-neutralizing Fab AbD09097.

Author information

Molecular Plant Physiology and Biophysics, Julius-von-Sachs Institute of the University Wuerzburg, Julius-von-Sachs Platz 2, 97082 Wuerzburg, Germany.
Life Science Group, Bio-Rad AbD Serotec, Zeppelinstrasse 4, 82178 Puchheim, Germany.


The secreted cystine-knot protein sclerostin was first identified from genetic screening of patients suffering from the rare bone-overgrowth diseases sclerosteosis and van Buchem disease. Sclerostin acts a negative regulator of bone growth through inhibiting the canonical Wnt signalling cascade by binding to and blocking the Wnt co-receptor LRP5/6. Its function in blocking osteoblastogenesis makes it an important target for osteoanabolic therapy approaches to treat osteoporosis, which is characterized by a progressive decrease in bone mass and density. In this work, the production, crystallization and preliminary X-ray diffraction data analysis of a sclerostin-neutralizing human Fab antibody fragment, AbD09097, obtained from a naive antibody library are reported. Crystals of the Fab AbD09097 belonged to space group P21, with unit-cell parameters a = 45.19, b = 78.49, c = 59.20 Å, β = 95.71° and diffracted X-rays to a resolution of 1.8 Å.


Wnt signalling pathway; bone homeostasis; osteoporosis; sclerostin

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center