Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks

The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein

Protein crystallographers are often confronted with recalcitrant proteins not readily crystallizable, or which crystallize in problematic forms. A variety of techniques have been used to surmount such obstacles: crystallization using carrier proteins or antibody complexes, chemical modification, surface entropy reduction, proteolytic digestion, and additive screening. Here we present a synergistic approach for successful crystallization of proteins that do not form diffraction quality crystals using conventional methods. This approach combines favorable aspects of carrier-driven crystallization with surface entropy reduction. We have generated a series of maltose binding protein (MBP) fusion constructs containing different surface mutations designed to reduce surface entropy and encourage crystal lattice formation. The MBP advantageously increases protein expression and solubility, and provides a streamlined purification protocol. Using this technique, we have successfully solved the structures of three unrelated proteins that were previously unattainable. This crystallization technique represents a valuable rescue strategy for protein structure solution when conventional methods fail.

/pdf/a-synergistic-approach-to-protein-crystallization-26q5df2kkd.pdf

A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.

Human cytomegalovirus (HCMV) poses a significant threat to immunocompromised individuals and neonates infected in utero. Glycoprotein B (gB), the herpesvirus fusion protein, is a target for neutralizing antibodies and a vaccine candidate due to its indispensable role in infection. Here we show the crystal structure of the HCMV gB ectodomain bound to the Fab fragment of 1G2, a neutralizing human monoclonal antibody isolated from a seropositive subject. The gB/1G2 interaction is dominated by aromatic residues in the 1G2 heavy chain CDR3 protruding into a hydrophobic cleft in the gB antigenic domain 5 (AD-5). Structural analysis and comparison with HSV gB suggest the location of additional neutralizing antibody binding sites on HCMV gB. Finally, immunoprecipitation experiments reveal that 1G2 can bind to HCMV virion gB suggesting that its epitope is exposed and accessible on the virus surface. Our data will support the development of vaccines and therapeutic antibodies against HCMV infection.

/pdf/structure-of-hcmv-glycoprotein-b-in-the-postfusion-36nhm6c4qy.pdf

Structure of HCMV glycoprotein B in the postfusion conformation bound to a neutralizing human antibody

Multivalency in the assembly of intrinsically disordered Dynein intermediate chain.

/pdf/in-situ-proteolysis-for-protein-crystallization-and-2rg4flc5l9.pdf

In situ proteolysis for protein crystallization and structure determination

Crystal structure of tetR-family transcriptional regulator

Cryptosporidium parvum putative polyprenyl pyrophosphate synthase (cgd4_2550) in complex with zoledronate

Crystal structure of human Dimethyladenosine transferase

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Papers

In situ proteolysis for protein crystallization and structure determination

Crystal structure of tetR-family transcriptional regulator

Cryptosporidium parvum putative polyprenyl pyrophosphate synthase (cgd4_2550) in complex with zoledronate

Crystal structure of human Dimethyladenosine transferase