IUCrBio

The aggregation process and the fibril state of an amyloidogenic peptide suggest monomer addition to be the prevailing mechanism of elongation and a model of the peptide packing in the fibrils has been obtained.

A review and historical perspective covering the many different aspects of antiparasitic drug discovery, in particular targeting protists, is presented. The key role of structural studies in the process is highlighted and specific high-profile examples are given.

The crystal structure of anti-influenza antibody CH65 at 1.70 Å resolution reveals that the affinity-matured antibody evolved to preconfigure the antibody loops to increase binding affinity to the hemagglutinin.

A comprehensive and up-to-date review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes is reported. Recent applications of the method for in situ serial crystallography at X-ray free-electron lasers and synchrotrons are described.

This article describes the structure determination of a membrane protein by serial injection of microcrystals in lipidic cubic phases into a synchrotron microfocus beam. The method is discussed with respect to serial femtosecond crystallography at free-electron lasers.

Two X-ray structures of APLP1 E2 with and without a heparin dodecasaccharide are presented, revealing two distinct binding modes of the protein to heparan sulfate. The data provide a mechanistic explanation of how APP-like proteins bind to heparan sulfates and how they specifically recognize nonreducing structures of heparan sulfates.

The structure of the giant haemoglobin from G. paulistus was determined.

A neutron crystallographic study of perdeuterated transthyretin reveals important aspects of the structure relating to its stability and its propensity to form fibrils, as well as evidence of a single water molecule that affects the symmetry of the two binding pockets.

Bragg diffraction achieved from two-dimensional protein crystals using femtosecond X-ray laser snapshots is presented.

The room-temperature structure of lysozyme is determined using 40000 individual diffraction patterns from micro-crystals flowing in liquid suspension across a synchrotron microfocus beamline.

High-dose serial femtosecond crystallography experiments were performed on microcrystals of the metalloprotein ferredoxin. Indications of radiation damage to the two [4Fe-4S] clusters are observed.