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 Å, b = 166.5 Å and c = 332.7 Å. The asymmetric unit seems to contain eight molecules of α-amylase, with crystal volume per protein mass (Vm) of 2.69 Å3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 Å 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 Å 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 |
| Publication status | Published - 1993 Dec 1 |
| Externally published | Yes |
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Keywords
- α-amylase
- Bacillus subtilis
- Crystallization
- Preliminary X-ray analysis
- X-ray crystallography
ASJC Scopus subject areas
- Virology
Cite this
Crystallization and preliminary X-ray crystallographic analysis of α-amylase from Bacillus subtilis. / Chang, Changsoo; Kim, Kyeong Kyu; Hwang, Kwang Yeon; Choi, Myung Un; Suh, Se Won.
In: Journal of Molecular Biology, Vol. 229, No. 1, 01.12.1993, p. 235-238.Research output: Contribution to journal › Article
}
TY - JOUR
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 - 1993/12/1
Y1 - 1993/12/1
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 Å, b = 166.5 Å and c = 332.7 Å. The asymmetric unit seems to contain eight molecules of α-amylase, with crystal volume per protein mass (Vm) of 2.69 Å3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 Å 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 Å 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 Å, b = 166.5 Å and c = 332.7 Å. The asymmetric unit seems to contain eight molecules of α-amylase, with crystal volume per protein mass (Vm) of 2.69 Å3/Da and solvent content of 54.3% by volume. Despite a very long c-axis, the crystals diffracted to about 2.2 Å 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 Å Bragg spacing from a native crystal.
KW - α-amylase
KW - Bacillus subtilis
KW - Crystallization
KW - Preliminary X-ray analysis
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=0027514707&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027514707&partnerID=8YFLogxK
M3 - Article
C2 - 8421303
AN - SCOPUS:0027514707
VL - 229
SP - 235
EP - 238
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -