X-ray crystallography

X-ray crystallography is a technique that uses X-ray diffraction patterns to determine high-resolution, three-dimensional structures of molecules such as proteins, small organic molecules, and materials. The substance of interest must be in crystalline form, which typically requires testing various crystallization conditions.

Latest Research and Reviews

  • Research
    | Open Access

    U2AF1 binds to the 3’ splice site of introns and its mutation lead to abnormal splicing. Here the authors solve the crystal structures of wild type and pathogenic mutant U2AF1 bound to target RNA, showing that different target sequence is preferred by pathogenic mutant.

    • Hisashi Yoshida
    • , Sam-Yong Park
    • , Gyosuke Sakashita
    • , Yuko Nariai
    • , Kanako Kuwasako
    • , Yutaka Muto
    • , Takeshi Urano
    •  & Eiji Obayashi
  • Research
    | Open Access

    Crystal structures of nucleosome fibres assembled from cohesive-ended dinucleosomes with and without linker histone reveal open zigzag conformations that are interdigitated with one another, and suggest the role that linker DNA plays in observed variable fibre configurations and packing.

    • Zenita Adhireksan
    • , Deepti Sharma
    • , Phoi Leng Lee
    •  & Curt A. Davey
  • Research
    | Open Access

    Neisseria meningitidis capsular polysaccharide (CPS) is a major virulence factor and vaccine formulations against Neisseria meningitidis serogroup A (NmA) contain O-acetylated CPS. Here, the authors provide mechanistic insights into CPS O-acetylation in NmA by determining the crystal structure of the O-acetyltransferase CsaC and NMR measurements further reveal that the CsaC-mediated reaction is regioselective for O3 and that the O4 modification results from spontaneous O-acetyl migration.

    • Timm Fiebig
    • , Johannes T. Cramer
    • , Andrea Bethe
    • , Petra Baruch
    • , Ute Curth
    • , Jana I. Führing
    • , Falk F. R. Buettner
    • , Ulrich Vogel
    • , Mario Schubert
    • , Roman Fedorov
    •  & Martina Mühlenhoff
  • Research
    | Open Access

    Schuhmacher, Beldar et al. design a super-substrate peptide based on the substrate sequence specificity of the SETD2 protein lysine methyltransferase. SETD2 methylates this super-substrate 290-fold more efficiently than the original H3K36 peptide. This study illustrates that substrate sequence design can improve the activity of protein lysine methyltransferases.

    • Maren Kirstin Schuhmacher
    • , Serap Beldar
    • , Mina S. Khella
    • , Alexander Bröhm
    • , Jan Ludwig
    • , Wolfram Tempel
    • , Sara Weirich
    • , Jinrong Min
    •  & Albert Jeltsch
  • Research |

    Rossjohn, van der Vliet and colleagues develop single-domain antibodies binding composite CD1d and NKT T-cell receptor antigens, inducing specific antitumor immune subsets.

    • Roeland Lameris
    • , Adam Shahine
    • , Daniel G. Pellicci
    • , Adam P. Uldrich
    • , Stephanie Gras
    • , Jérôme Le Nours
    • , Richard W. J. Groen
    • , Jana Vree
    • , Scott J. J. Reddiex
    • , Sergio M. Quiñones-Parra
    • , Stewart K. Richardson
    • , Amy R. Howell
    • , Sonja Zweegman
    • , Dale I. Godfrey
    • , Tanja D. de Gruijl
    • , Jamie Rossjohn
    •  & Hans J. van der Vliet
  • Research |

    A chemoenzymatic method to site-specifically conjugate peptide and protein thioesters to folded proteins at lysine residues has been developed. The method uses a genetically encoded four-residue tag that is recognized by the E2 SUMO-conjugating enzyme Ubc9. This approach enables isopeptide formation with just Ubc9 in a programmable manner and obviates the need for E1 and E3 enzymes.

    • Raphael Hofmann
    • , Gaku Akimoto
    • , Thomas G. Wucherpfennig
    • , Cathleen Zeymer
    •  & Jeffrey W. Bode

News and Comment

  • News and Views |

    The enzyme 5-lipoxygenase (5-LOX) initiates the biosynthesis of leukotrienes (LT), potent mediators of the inflammatory response. The first crystal structures of two complexes of inhibitor bound to 5-LOX reveal the functional consequences of the binding, including a change in the regiospecificity toward a 12/15-lipoxygenating enzyme.

    • Homero Rubbo
    •  & Irene Wood
  • News and Views |

    A suite of new enzymes reveals more on how Nature breaks down plant-based polysaccharides and how these enzymes might be harnessed in the utilization of plant-based biomass.

    • Paul H. Walton
  • Comments and Opinion
    | Open Access

    Amid the COVID-19 pandemic, scientists around the globe have been working resolutely to find therapies to treat patients and avert the spreading of the SARS-CoV-2 virus. In this commentary, we highlight some of the latest studies that provide atomic-resolution structural details imperative for the development of vaccines and antiviral therapeutics.

    • Yi Zhang
    •  & Tatiana G. Kutateladze
  • News and Views |

    The discovery of selective modulators of two Cryptochrome isoforms, CRY1 and CRY2, permits a deeper understanding of how circadian clock proteins impact diverse aspects of our daily 24-h rhythms and how this intersects with metabolic pathways relevant to disease.

    • Julia Lara
    •  & Brian D. Zoltowski
  • News and Views |

    Oxygen activation mechanisms catalyzed by flavin cofactors are established for electron transfer (oxidases) and C4a covalent flavin–oxygen adduct formation (oxygen-inserting monooxygenases). A new paradigm for oxygen insertion involving a flavin-N5-aminoperoxide intermediate has now been discovered in select flavin-dependent monooxygenases.

    • David Leys
    •  & Nigel S. Scrutton