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

doi:10.1006/jmbi.1993.1020

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 journal › Article › peer-review

3 Citations (Scopus)

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 (V_m) 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
Pages (from-to)	235-238
Number of pages	4
Journal	Journal of Molecular Biology
Volume	229
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.1993.1020
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

Structural Biology
Molecular Biology

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title = "Crystallization and preliminary X-ray crystallographic analysis of α-amylase from Bacillus subtilis",

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 A{\AA}, b = 166.5 A{\AA} and c = 332.7 A{\AA}. The asymmetric unit seems to contain eight molecules of α-amylase, with crystal volume per protein mass (Vm) of 2.69 A{\AA}3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 A{\AA} 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{\AA} Bragg spacing from a native crystal.",

keywords = "Bacillus subtilis, Crystallization, Preliminary X-ray analysis, X-ray crystallography, α-amylase",

author = "Changsoo Chang and Kim, {Kyeong Kyu} and Hwang, {Kwang Yeon} and Choi, {Myung Un} and Suh, {Se Won}",

year = "1993",

month = jan,

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doi = "10.1006/jmbi.1993.1020",

language = "English",

volume = "229",

pages = "235--238",

journal = "Journal of Molecular Biology",

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T1 - Crystallization and preliminary X-ray crystallographic analysis of α-amylase from Bacillus subtilis

AU - Chang, Changsoo

AU - Kim, Kyeong Kyu

AU - Hwang, Kwang Yeon

AU - Choi, Myung Un

AU - Suh, Se Won

PY - 1993/1/5

Y1 - 1993/1/5

N2 - 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.

AB - 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.

KW - Bacillus subtilis

KW - Crystallization

KW - Preliminary X-ray analysis

KW - X-ray crystallography

KW - α-amylase

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

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Keywords

ASJC Scopus subject areas

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