Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis

Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and overexpressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C222(1), with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 Angstrom and with one molecule of spsA. in the asymmetric unit. The crystals diffract beyond 1.5 Angstrom using synchrotron radiation.