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Crystallization and preliminary X-ray diffraction studies of an alkaline protease from Bacillus lentus

1988; Elsevier BV; Volume: 204; Issue: 3 Linguagem: Inglês

10.1016/0022-2836(88)90372-5

1089-8638

Christian Betzel, Zbigniew Dauter, Mirosława Dauter, Margareta Ingelman, Gerlind Papendorf, Keith S. Wilson, Sven Branner,

Protein Structure and Dynamics

Various crystal forms of the subtilisin-type protease Savinase (EC 3.4.21.14) from the alkalophilic bacterium Bacillus lentus have been obtained. The first were orthorhombic needles, space group P212121, with unit cell dimensions a = 75.3 Å, b = 53.4 Å, c = 61.5 Å. The crystals diffract to at least 1.8 Å resolution, and the data to 2.0 Å have been recorded on film using synchrotron radiation. The second crystal form grows as similar orthorhombic needles, also in P212121, with cell dimensions a = 75.5 Å, b = 47.4 Å, c = 62.5 Å, mainly differing from the first in the shorter b-axis. Data have been recorded to 2.8 Å. The third form is monoclinic, space group P21 with dimensions a = 40.7 Å, b = 64.4 Å, c = 43.0 Å, β = 119 °. Data to a spacing of 2.4 Å have been recorded for this form.