Printed in U.S.A. Crystallization and Preliminary Analysis of Crystals of Apolipophorin I11 Isolated from Locusta migratoria”

Crystals of apolipophorin 111, isolated from the locust Locusta migratoria, have been reproducibly grown from ammonium sulfate solutions and are well suited for an x-ray crystallographic analysis. Locust apoli-pophorin 111 is a glycosylated protein with a molecular weight of 19,100 and interacts with lipophorin, the major lipoprotein complex in insects. The crystals be-long to the space group P6+?2 or P6a22 owwith unit cell dimensions of a = b = 67.5 A, c 7 155.6 A and diffract to a nominal resolution of 2.5 A. They are physically robust and are stable in the x-ray beam for over a week. A complete native x-Tay data set has been col-lected and processed to 3.0-A resolution. In some insect orders such as Lepidoptera and Orthoptera P-oxidation of fatty acids serves as the source of fuel fo