draft crystal structure of the vault shell at 9-？ resolution草案的晶体结构拱顶在9 -壳决议.pdfVIP

PLoS BIOLOGY Draft Crystal Structure of the ˚ Vault Shell at 9-A Resolution 1 2,3 4 2,3 1,2,3,* Daniel H. Anderson , Valerie A. Kickhoefer , Stuart A. Sievers , Leonard H. Rome , David Eisenberg 1 Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, California, United States of America, 2 Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, United States of America, 3 California NanoSystems Institute, University of California Los Angeles, Los Angeles, California, United States of America, 4 Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, California, United States of America Vaults are the largest known cytoplasmic ribonucleoprotein structures and may function in innate immunity. The vault shell self-assembles from 96 copies of major vault protein and encapsulates two other proteins and a small RNA. We crystallized rat liver vaults and several recombinant vaults, all among the largest non-icosahedral particles to have been crystallized. The best crystals thus far were formed from empty vaults built from a cysteine-tag construct of major ˚ vault protein (termed cpMVP vaults), diffracting to about 9-A resolution. The asymmetric unit contains a half vault of molecular mass 4.65 MDa. X-ray phasing was initiated by molecular replacement, using density from cryo-electron microscopy (cryo-EM). Phases were improved by density modification, includin