Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside.
- 1 February 2000
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 127 (2) , 181-184
- https://doi.org/10.1093/oxfordjournals.jbchem.a022592
Abstract
The cell surface antigen CD38 is a multifunctional ectoenzyme that acts as an NAD+ glycohydrolase, an ADP-ribosyl cyclase, and also a cyclic ADP-ribose hydrolase. The extracellular catalytic domain of CD38 was expressed as a fusion protein with maltose-binding protein, and was crystallized in the complex with a ganglioside, GTlb, one of the possible physiological inhibitors of this ectoenzyme. Two different crystal forms were obtained using the hanging-drop vapor diffusion method with PEG 10,000 as the precipitant. One form diffracted up to 2.4 Å resolution with synchrotron radiation at 100 K, but suffered serious X-ray damage. It belongs to the space group P212121 with unit-cell parameters of a = 47.9, b = 94.9, c = 125.2 Å. The other form is a thin plate, but the data sets were successfully collected up to 2.4 Å resolution by use of synchrotron radiation at 100 K. The crystals belong to the space group P21 with unit-cell parameters of a = 57.4, b = 51.2, c = 101.1 Å, and α = 97.9°, and contain one molecule per asymmetric unit with a VM value of 2.05 Å3/Da.Keywords
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