Tags

Type your tag names separated by a space and hit enter

Crystallization and preliminary X-ray crystallographic analysis of alpha-amylase from Bacillus subtilis.
J Mol Biol. 1993 Jan 05; 229(1):235-8.JM

Abstract

Large crystals of alpha-amylase from Bacillus subtilis have been obtained at room temperature using polyethylene glycol 6000 as precipitant. They grow to typical dimensions of 0.25 mm x 0.3 mm x 2.0 mm in five days. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 85.46 A, b = 166.5 A and c = 332.7 A. The asymmetric unit seems to contain eight molecules of alpha-amylase, with crystal volume per protein mass (Vm) of 2.69 A3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 A 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 A Bragg spacing from a native crystal.

Links

Publisher Full Text

Authors+Show Affiliations

Chang C
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Kim KK
No affiliation info available
Hwang KY
No affiliation info available
Choi MU
No affiliation info available
Suh SW
No affiliation info available

MeSH

Bacillus subtilisCrystallizationX-Ray Diffractionalpha-Amylases

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8421303

Citation

Chang, C, et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of Alpha-amylase From Bacillus Subtilis." Journal of Molecular Biology, vol. 229, no. 1, 1993, pp. 235-8.
Chang C, Kim KK, Hwang KY, et al. Crystallization and preliminary X-ray crystallographic analysis of alpha-amylase from Bacillus subtilis. J Mol Biol. 1993;229(1):235-8.
Chang, C., Kim, K. K., Hwang, K. Y., Choi, M. U., & Suh, S. W. (1993). Crystallization and preliminary X-ray crystallographic analysis of alpha-amylase from Bacillus subtilis. Journal of Molecular Biology, 229(1), 235-8.
Chang C, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of Alpha-amylase From Bacillus Subtilis. J Mol Biol. 1993 Jan 5;229(1):235-8. PubMed PMID: 8421303.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic analysis of alpha-amylase from Bacillus subtilis. AU - Chang,C, AU - Kim,K K, AU - Hwang,K Y, AU - Choi,M U, AU - Suh,S W, PY - 1993/1/5/pubmed PY - 1993/1/5/medline PY - 1993/1/5/entrez SP - 235 EP - 8 JF - Journal of molecular biology JO - J Mol Biol VL - 229 IS - 1 N2 - Large crystals of alpha-amylase from Bacillus subtilis have been obtained at room temperature using polyethylene glycol 6000 as precipitant. They grow to typical dimensions of 0.25 mm x 0.3 mm x 2.0 mm in five days. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 85.46 A, b = 166.5 A and c = 332.7 A. The asymmetric unit seems to contain eight molecules of alpha-amylase, with crystal volume per protein mass (Vm) of 2.69 A3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 A 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 A Bragg spacing from a native crystal. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8421303/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_alpha_amylase_from_Bacillus_subtilis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71020-X DB - PRIME DP - Unbound Medicine ER -