X-ray crystallography articles within Nature

Featured

  • Letter |

    Structural and functional analysis of the centralspindlin complex shows that it connects the mitotic spindle to the plasma membrane during cytokinesis through interactions of the C1 domain of centralspindlin’s MgcRacGAP subunit with phosphoinositide lipids.

    • Sergey Lekomtsev
    • , Kuan-Chung Su
    •  & Mark Petronczki

  • Article |

    The X-ray crystal structure of the human G-protein-coupled receptor protease-activated receptor 1 (PAR1) bound to the antagonist vorapaxar is solved, revealing an unusual method of drug binding that should facilitate the development of improved PAR1-selective antagonists.

    • Cheng Zhang
    • , Yoga Srinivasan
    •  & Brian K. Kobilka

  • Article |

    An X-ray crystal structure of the bacterial cellulose synthase captures the process of cellulose synthesis and membrane translocation; the structure indicates how the synthesis of cellulose and the translocation of the nascent polysaccharide chain across the cell membrane are coupled.

    • Jacob L. W. Morgan
    • , Joanna Strumillo
    •  & Jochen Zimmer

  • Books & Arts |

    Philip Ball is gripped by the life of a remarkable scientist whose flawed theory dented her reputation.

    • Philip Ball

  • Article |

    The twin-arginine translocation (Tat) pathway transports folded proteins across membranes in bacteria and plant chloroplasts; the crystal structure of TatC, an integral membrane protein and core component of this complex, is now presented.

    • Sarah E. Rollauer
    • , Michael J. Tarry
    •  & Susan M. Lea

  • Letter |

    Crystal structures of the Pol II–TFIIB complex in free form and bound by the DNA template and a short RNA product are reported; the latter complex represents an initially transcribing complex, a critical transient state in the pathway from transcription initiation to elongation.

    • Sarah Sainsbury
    • , Jürgen Niesser
    •  & Patrick Cramer

  • Comment |

    A century ago this week, physicist Lawrence Bragg announced an equation that revolutionized fields from mineralogy to biology, writes John Meurig Thomas.

    • John Meurig Thomas

  • Letter |

    The crystal structure of the Mediator head module from the fission yeast Schizosaccharomyces pombe is solved at 3.4 Å resolution.

    • Laurent Larivière
    • , Clemens Plaschka
    •  & Patrick Cramer

  • Obituary |

    Crystallographer who pioneered methods of X-ray imaging and modern computing.

    • Janos Kirz
    •  & Jianwei Miao

  • Outlook |

    X-ray crystallographer currently at the Weizmann Institute of Science in Rehovot, Israel. She won a share of the 2009 Nobel Prize in Chemistry for her work on the structure and function of the ribosome. Yonath was born in 1939 in Jerusalem to a poor family. Her father died when she was 11 years old, and Yonath helped support her mother and younger sister. Yonath was the first Israeli woman to win a Nobel prize and the first woman in 45 years to win the Nobel Prize in Chemistry

    • Ada Etil Yonath

  • Letter |

    The start-up of the new femtosecond hard X-ray laser facility in Stanford, the Linac Coherent Light Source, has brought high expectations for a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. This new capability is tested for the problem of structure determination from nanocrystals of macromolecules that cannot be grown in large crystals. Over three million diffraction patterns were collected from a stream of nanocrystals of the membrane protein complex photosystem I, which allowed the assembly of a three-dimensional data set for this protein, and proves the concept of this imaging technique.

    • Henry N. Chapman
    • , Petra Fromme
    •  & John C. H. Spence

  • Letter |

    The E1 and E2 glycoproteins of alphaviruses form heterodimers and assemble into spikes on the virus surface, which mediate receptor binding and endocytosis. When the virion encounters acidic pH in the endosome E1 and E2 dissociate and E1 triggers fusion with the endosomal membrane. Two papers now provide the first crystal structures for glycoprotein complexes incorporating E2 at acidic and neutral pH, respectively. Together they provide insight into how fusion activation is controlled in alphaviruses.

    • James E. Voss
    • , Marie-Christine Vaney
    •  & Félix A. Rey

  • Books & Arts |

    Josie Glausiusz enjoys a play capturing the zeal and backstabbing in the race to discover DNA's structure.

    • Josie Glausiusz

  • Letter |

    Insertion of retrovirus genome into host genome to replicate is mediated by a tetramer of the virus-encoded integrase protein. The structure of a related integrase from prototype foamy virus bound to the cleaved viral DNA ends, a complex called the intasome, was previously revealed. These authors solve the structure of the intasome interacting with the target host DNA both before and after it is cleaved, revealing new details of the integration process that may help in designing improved inhibitors of HIV.

    • Goedele N. Maertens
    • , Stephen Hare
    •  & Peter Cherepanov

  • Letter |

    Natural killer cells and cytotoxic T cells kill virus-infected and malignant cells, releasing the pore-forming protein perforin in the process. Perforin is required for the delivery of pro-apoptotic granzymes to the target cell. These authors present the crystal structure of a perforin monomer together with a cryo-electron microscopy reconstruction of the oligomeric pore. Perforin monomers within the pore are arranged with an inside-out orientation relative to the structurally homologous monomers of cholesterol-dependent cytolysins.

    • Ruby H. P. Law
    • , Natalya Lukoyanova
    •  & James C. Whisstock

  • Letter |

    Propionyl-coenzyme A carboxylase (PCC) is a biotin-dependent enzyme that is essential for the catabolism of several amino acids, cholesterol and some fatty acids. Here, the crystal structure of a bacterial PCC is presented, along with a cryo-electron microscopy reconstruction showing a similar structure for human PCC. The structural information establishes a molecular basis for understanding the known disease-causing mutations in PCC, and is relevant to the holoenzymes of other biotin-dependent carboxylases.

    • Christine S. Huang
    • , Kianoush Sadre-Bazzaz
    •  & Liang Tong

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