Crystallization and preliminary X-ray crystallographic analysis of squalene-hopene cyclase from Alicyclobacillus acidocaldarius.
The membrane-associated protein squalene-hopene cyclase from Alicyclobacillus acidocaldarius was overexposed in Escherichia coli and purified by ion exchange and gel permeation chromatography. Crystals of three interrelated forms were grown by vapor diffusion under identical conditions. The crystals diffract to about 2.3 A resolution, but they are unstable in the X-ray beam. An interpretable heavy-atom derivative was obtained.
Wendt
K U
KU
Institut für Chemie und Biochemie, Freiburg im Breisgau, Germany.
Feil
C
C
Lenhart
A
A
Poralla
K
K
Schulz
G E
GE
D001406:Bacillaceae / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D007535:Isomerases; D019751:Intramolecular Transferases; C066630:squalene-hopene cyclase