Crystallization and preliminary crystallographic analysis of Streptomyces griseus aminopeptidase.
Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E. Sigma) and single crystals were obtained by the vapor diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P4(1)2(1)2 (P4(3)2(1)2), with cell dimensions of a = b = 61.82(3) A and c = 145.88(4) A. These crystals are mechanically strong, they are stable in the X-ray beam and they diffract to better than 1.8 A resolution. The cell dimensions and the cell symmetry are consistent with one molecule in the asymmetric unit and the crystals are suitable for a detailed high-resolution crystallographic analysis. A complete native data set to 1.9 A resolution has been collected on a Rigaku R-AXIS-IIC Imaging Plate Detector system and a heavy-atom derivative search is in progress.
Almog
O
O
Department of Inorganic Chemistry, Hebrew University of Jerusalem, Israel.
Greenblatt
H M
HM
Spungin
A
A
Ben-Meir
D
D
Blumberg
S
S
Shoham
G
G
D000626:Aminopeptidases / Q000737:chemistry* / Q000648:ultrastructure; D003461:Crystallography; D013305:Streptomyces griseus / Q000201:enzymology*
D000626:Aminopeptidases