Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin.
Ecotin, a novel serine protease inhibitor isolated from Escherichia coli, has been crystallized using polyethylene glycol 1500 as the precipitating agent. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters of a = 39.22 A, b = 84.86 A, and c = 98.74 A. The asymmetric unit contains one dimeric molecule of ecotin, with a crystal volume per protein mass (Vm) of 2.55 A3/Da and a solvent content of 51.8% by volume. The crystals diffract to at least 2.2 A using a conventional X-ray source, and X-ray data have been collected to 2.7 A Bragg spacing from a native crystal.
Shin
D H
DH
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Hwang
K Y
KY
Kim
K K
KK
Lee
H R
HR
Lee
C S
CS
Chung
C H
CH
Suh
S W
SW
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D011480:Protease Inhibitors / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; C039076:Eco protein, E coli; D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D011480:Protease Inhibitors