A truncated β-amylase (E.C. 18.104.22.168) from Bacillus polymyxa has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals belong to the orthorhombic space group P212121 with cell dimensions a = 64.6, b = 141.9, c = 155.1 Å and diffract to 2.5 Å resolution. The asymmetric unit containing three protein molecules was derived from an electron-density map calculated at 4 Å resolution using MIR phases. This gives a V(m) value of 2.36 Å3 Da-1.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 1999 Apr 1|
ASJC Scopus subject areas
- Structural Biology