Crystallization and preliminary analysis of crystals of apolipophorin III isolated from Locusta migratoria.
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.
Holden
H M
HM
Department of Biochemistry, University of Arizona, Tucson 85721.
Kanost
M R
MR
Law
J H
JH
Rayment
I
I
Wells
M A
MA
D000818:Animals; D001053:Apolipoproteins / Q000302:isolation & purification; D002352:Carrier Proteins; D003460:Crystallization; D006110:Grasshoppers / Q000378:metabolism*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001053:Apolipoproteins; D002352:Carrier Proteins; C042470:apolipophorin III