Crystal growth and preliminary X-ray study of glutamic acid specific serine protease from Bacillus intermedius

The glutamic acid specific protease (glutamyl-endopeptidase) from Bacillus intermedius, strain 3-19, was isolated and purified using ion exchange chro matography on CM-cellulose and Mono-S FPLC column. The conditions for cryst allization of the enzyme have been discussed. The crystals of enzyme were g rown using hanging-drop vapor-diffusion technique. Crystals belong to the s pace group C2 with unit cell parameters of a = 61.62 Angstrom, b = 55.84 An gstrom, c = 60.40 Angstrom, beta = 117.6 degrees X-ray diffraction data to 1.68 Angstrom resolution were collected using synchrotron radiation (EMBL, Hamburg) and an imaging plate scanner. (C) 1999 Elsevier Science B.V. All r ights reserved.