Crystallization and preliminary X-ray structure determination of Lupinus luteus PR10 protein

The pathogenesis-related protein of the PR10 class from Lupinus luteus (yel low lupin), L1PR10.1A, is constitutively expressed in roots. It is also acc umulated in leaves treated with a suspension of pathogenic bacteria as a re sponse to stress. Recombinant yellow-lupin L1PR10.1A protein has been overe xpressed in Escherichia coli as a fusion product with maltose-binding prote in. L1PR10.1A crystallizes in the orthorhombic P2(1)2(1)2(1) space group an d the crystals diffract to 2.45 Angstrom resolution. The structure has been solved by molecular replacement, using the structure of a birch-pollen all ergen protein as a model.