Crystallization and preliminary X-ray investigation of proteinase A, a non-pepsin-type acid proteinase from Aspergillus niger var. macrosporus.
Proteinase A from Aspergillus niger var. macrosporus is a non-pepsin-type acid proteinase distinctly different in various properties from the family of pepsin-type aspartic proteinases, and so far it remains unknown which residues participate in the catalysis of the enzyme and how the mechanism operates. The acid proteinase A was crystallized from an ammonium sulfate solution by the hanging-drop vapor diffusion method. The space group of the crystals was P2(1)2(1)2(1) with unit cell dimensions of a = 54.7 A, b = 70.4 A and c = 38.0 A. On the assumption that there is one enzyme molecule in the asymmetric unit, the calculated ratio of volume to unit protein mass (Vm) was 1.64 A3 per dalton. Diffraction data were collected up to a resolution higher than 1.5 A, using the Weissenberg camera for macromolecular crystallography with synchrotron radiation. The crystal of proteinase A is, therefore, suitable for the structural analysis with a high resolution.
Tanokura
M
M
Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo, Japan.
Matsuzaki
H
H
Iwata
S
S
Nakagawa
A
A
Hamaya
T
T
Takizawa
T
T
Takahashi
K
K
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D001230:Aspergillus / Q000201:enzymology*; D003461:Crystallography; D011487:Protein Conformation; D014961:X-Ray Diffraction
C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases