Crystallization and preliminary crystallographic analysis of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix.
Crystals of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix strain K1 have been grown at 291 K using ammonium phosphate as a precipitant. The diffraction pattern of the crystal extends to 2.4 A resolution at 100 K using Cu Kalpha radiation. The crystal belongs to space group P1, with unit-cell parameters a = 107.5, b = 109.9, c = 119.4 A, alpha = 108.1, beta = 109.8, gamma = 91.9 degrees. The presence of eight molecules per asymmetric unit gives a crystal volume per protein mass (V(M)) of 2.4 A(3) Da(-1) and a solvent content of 48% by volume. A full set of X-ray diffraction data was collected to 2.9 A from the native crystal.
Wang
Ganggang
G
MOE Laboratory of Protein Science and Laboratory of Structural Biology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Gao
Renjun
R
Ding
Yi
Y
Yang
Haitao
H
Cao
Shugui
S
Feng
Yan
Y
Rao
Zihe
Z
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019620:Desulfurococcaceae / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000737:chemistry*; D011487:Protein Conformation
D019843:Archaeal Proteins; D010447:Peptide Hydrolases; C038220:acylaminoacyl-peptidase