Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum.
Single cystals of proteasomes from the archaebacterium Thermoplasma acidophilum were obtained using the hanging-drop vapor diffusion method. The crystals diffract to better than 3.0 A and belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 308.9 A, b = 208.8 A and c = 116.9 A. There is one molecular complex in the asymmetric unit. Two potentially useful heavy-atom derivatives have been obtained. The self-rotation function of the native Patterson map shows local sevenfold symmetry, consistent with the low-resolution structure obtained by electron microscopic techniques. The unit cell dimensions and crystal symmetry together with the shape and size of the proteasome suggest a packing arrangement of proteasome molecules in the unit cell, with their cylinder axis nearly parallel to the crystallographic a-axis.
Jap
B
B
Max-Planck-Institut für Biochemie, Martinsried bei München, Germany.
Pühler
G
G
Lücke
H
H
Typke
D
D
Löwe
J
J
Stock
D
D
Huber
R
R
Baumeister
W
W
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000302:isolation & purification; D046988:Proteasome Endopeptidase Complex; D011487:Protein Conformation; D013822:Thermoplasma / Q000201:enzymology*
D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex