Abstract
Large crystals of α-amylaae from Bacillus subtilis have been obtained at room temperature using polyethylene glycol 6000 as precipitant. They grow to typical dimensions of 0.25 mm × 0.3 mm × 2.0 mm in five days. The crystals belong to the orthorhombic space group P212121, with unit cell dimensions of a = 85.46 AÅ, b = 166.5 AÅ and c = 332.7 AÅ. The asymmetric unit seems to contain eight molecules of α-amylase, with crystal volume per protein mass (Vm) of 2.69 AÅ3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 AÅ Bragg spacing using the rotating anode X-rays and were resistant to damage by X-rays. Thus they are suitable for structure determination by X-ray methods at high resolution. X-ray diffraction data have been collected to 3.4 AÅ Bragg spacing from a native crystal.
Original language | English |
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Pages (from-to) | 235-238 |
Number of pages | 4 |
Journal | Journal of Molecular Biology |
Volume | 229 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1993 Jan 5 |
Externally published | Yes |
Keywords
- Bacillus subtilis
- Crystallization
- Preliminary X-ray analysis
- X-ray crystallography
- α-amylase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology