SIMBAD: a sequence-independent molecular-replacement pipeline

SIMBAD is a sequence-independent molecular-replacement pipeline for solving difficult molecular-replacement cases where contaminants have been crystallized. It can also be used to find structurally related search models where no obvious homologue can be found through sequence-based searching.

MR-REX: molecular replacement by cooperative conformational search and occupancy optimization on low-accuracy protein models

A new algorithm, MR-REX, has been developed to perform a molecular-replacement search through replica-exchange Monte Carlo simulations. The algorithm enables cooperative rotation and translation searches and simultaneous clash and occupancy optimization, and improves the success rate of molecular replacement on low-accuracy structure models.

From deep TLS validation to ensembles of atomic models built from elemental motions. II. Analysis of TLS refinement results by explicit interpretation

The values of anisotropic atomic displacement parameters (ADPs) that correspond to concerted motions can be obtained from refined TLS matrices analytically or numerically. The difference between the ADPs obtained using these two methods can be used to assess the results of TLS refinement.

Structure of the flavocytochrome c sulfide de­hydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxus ARh 1

The structure of the monohaem flavocytochrome c sulfide dehydrogenase co-purified and co-crystallized with the copper-binding protein CopC was solved and refined to 2.6 Å resolution.

Crystal structure of the spliceosomal DEAH-box ATPase Prp2

The DEAH-box ATPase Prp2 is a key player during pre-mRNA splicing. Here, the first four crystal structures of this spliceosomal factor are reported in two different states, and the flexibility of its C-terminal domains and a previously undescribed ADP conformation are reported.

Identifying G protein-coupled receptor dimers from crystal packings

Analysis of intermolecular interactions in the crystal structures of G protein-coupled receptors showed two major types of dimers.

Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction

The biochemical and crystallographic characterization of different Catharanthus roseus receptor kinase 1-like membrane receptors is reported as a first step to understand cell-wall sensing and signalling mechanisms in plants.

The structure of the C-terminal domain of the nucleoprotein from the Bundibugyo strain of the Ebola virus in complex with a pan-specific synthetic Fab

A high-resolution crystal structure of a pan-specific synthetic Fab selected using a phage-display system against the C-terminal domain of the nucleoprotein from the Ebola virus is reported.

A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease

The crystal structure of the complex between a substrate selected by phage display and the D25N variant of HIV-1 protease is reported at a resolution of 1.1 Å. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate.

Crystal structure of the FAS1 domain of the hyaluronic acid receptor stabilin-2

A high-resolution X-ray structure of the seventh FAS1 domain of stabilin-2 is presented. This structure provides the first insight into the structure of stabilin-2.

Engineering glycoside hydrolase stability by the introduction of zinc binding

The engineering of metal binding into a cellulase increases its temperature stability while maintaining its other catalytic properties.

Bror Erik Strandberg (1930–2018)

Bror Strandberg was one of the pioneers in protein and virus structure determination. He was one of the scientists who first worked on the high-resolution structure of myoglobin and went on to work with viruses.