Crystallization and preliminary X-ray crystallographic analysis of α-amylase from Bacillus subtilis

Changsoo Chang, Kyeong Kyu Kim, Kwang Yeon Hwang, Myung Un Choi, Se Won Suh

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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 languageEnglish
Pages (from-to)235-238
Number of pages4
JournalJournal of Molecular Biology
Issue number1
Publication statusPublished - 1993 Jan 5
Externally publishedYes


  • Bacillus subtilis
  • Crystallization
  • Preliminary X-ray analysis
  • X-ray crystallography
  • α-amylase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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