title: Crystallization and preliminary analysis of crystals of apolipophorin III isolated from Locusta migratoria.
abstract: Crystals of apolipophorin III, 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 apolipophorin III is a glycosylated protein with a molecular weight of 19,100 and interacts with lipophorin, the major lipoprotein complex in insects. The crystals belong to the space group P6122 or P6522 with unit cell dimensions of a = b = 67.5 A, c = 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-ray data set has been collected and processed to 3.0-A resolution.
authors.affiliation: Department of Biochemistry, University of Arizona, Tucson 85721.
authors.forename: H M
authors.initials: HM
authors.lastname: Holden
authors.forename: M R
authors.initials: MR
authors.lastname: Kanost
authors.forename: J H
authors.initials: JH
authors.lastname: Law
authors.forename: I
authors.initials: I
authors.lastname: Rayment
authors.forename: M A
authors.initials: MA
authors.lastname: Wells
mesh_terms: D000818:Animals; D001053:Apolipoproteins / Q000302:isolation & purification; D002352:Carrier Proteins; D003460:Crystallization; D006110:Grasshoppers / Q000378:metabolism*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D001053:Apolipoproteins; D002352:Carrier Proteins; C042470:apolipophorin III