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Updated: Aug 23, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Low-resolution X-ray diffraction data obtained from hexagonal crystals of methylamine-treated alpha2-macroglobulin
1Department of Chemistry, University of Aarhus, Denmark.
Abstract:
Two hexagonal crystal forms of tetrameric human methylamine-treated alpha(2)-macroglobulin have been grown by vapour diffusion. One of the crystal forms diffracts X-rays beyond 9 A resolution. The space group of this form is P6(2)22 or P6(4)22 with a = b = 327, c = 219 A and with one dimer of alpha(2)-macroglobulin in the asymmetric unit. Several data sets have been collected by the use of synchrotron radiation at cryogenic temperature. A native data set extending to 10 A resolution has been obtained. The merging R factor of these data is 10.3%.
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