Structure of the catalytic core module of the Chaetomium thermophilum family GH6 cellobio­hydrolase Cel6A

The three-dimensional structure of an industrially relevant cellulase in complex with ligands has been determined at a resolution of 1.9 Å.

Low-density crystal packing of human protein kinase CK2 catalytic subunit in complex with resorufin or other ligands: a tool to study the unique hinge-region plasticity of the enzyme without packing bias

A low-resolution structure of the catalytic subunit CK2α of human protein kinase CK2 (formerly known as casein kinase 2) in complex with the ATP-competitive inhibitor resorufin is presented. An overview of all published human CK2α crystal packings serves as the basis for a discussion of the factors that determine whether the open or the closed hinge/helix αD conformation is adopted.

Nanolitre-scale crystallization using acoustic liquid-transfer technology

Acoustic droplet ejection achieves precise, tipless, non-invasive transfer of diverse aqueous solutions, enabling nanolitre-scale crystallization trials. The rapid and scalable technique demonstrated successful crystal growth with diverse targets in drop volumes as small as 20 nl.

An engineered PII protein variant that senses a novel ligand: atomic resolution structure of the complex with citrate

A mutant variant of the Synechococcus elongatus PII protein (PII-I86N) has been identified to have impaired 2-­oxoglutarate binding. Here, the PII-I86N variant was cocrystallized in the presence of ATP, magnesium and citrate and its structure was solved at a resolution of 1.05 Å.

The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences

O-Acetylserine sulfhydrylase (OASS) from L. donovani can bind to serine acetyltransferase (SAT) C-terminus mimicking peptides with a range of bulkiness; the strength of these interactions correlates with the size of the peptide side chains and the size of the active-site cleft. Differences in the interactions of OASS and SAT from various species may be explained by the size of the active-site cleft.

Structures of the γ-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch

Crystal structures of YrdA from E. coli show conformations that have not been reported for γ-class carbonic anhydrase family proteins.

Structural plasticity of tubulin assembly probed by vinca-domain ligands

The structure of ustiloxin D bound to tubulin was determined at a resolution which allows interatomic interactions to be defined and provides a basis for the structure-based design of ligands with improved activity. It is also shown how local interactions of vinca-domain ligands with tubulin influence the relative positioning of the latter and lead to the large-scale polymorphism of ligand-mediated tubulin assemblies.

Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX

All-atom models derived from moderate-resolution protein crystal structures contain a high frequency of close nonbonded contacts, independent of the major refinement program used for structure determination. All-atom refinement with PrimeX corrects many of these problematic interactions, producing models that are better suited for use in computational chemistry and related applications.

Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold

The structure of the C-terminal domain of yCdc73 revealed a GTPase-like fold.

The PAD region in the mycobacterial DinB homologue MsPolIV exhibits positional heterogeneity

The structure of a Y-family DNA polymerase from Mycobacteria named MsDpo4 along with solution studies suggest that the PAD region is endowed with the ability to adopt multiple orientations. This attribute would allow the enzyme to accommodate alterations in the width of the DNA double helix to facilitate its twin functions of trans-lesion bypass and adaptive mutagenesis.

X-ray structure of Salmonella typhimurium uridine phosphorylase complexed with 5-fluorouracil and molecular modelling of the complex of 5-fluorouracil with uridine phosphorylase from Vibrio cholerae

X-ray structures and in silico models are reported for complexes of the drug 5-fluorouracil with uridine phosphorylases from S. typhimurium and V. cholerae.

The use of workflows in the design and implementation of complex experiments in macromolecular crystallography

A powerful and easy-to-use workflow environment has been developed at the ESRF for combining experiment control with online data analysis on synchrotron beamlines. This tool provides the possibility of automating complex experiments without the need for expertise in instrumentation control and programming, but rather by accessing defined beamline services.

RCrane: semi-automated RNA model building

RCrane is a new tool for the partially automated building of RNA crystallographic models into electron-density maps of low or intermediate resolution. This tool helps crystallographers to place phosphates and bases into electron density and then automatically predicts and builds the detailed all-atom structure of the traced nucleotides.

Structure of the branched-chain aminotransferase from Streptococcus mutans

The crystal structure of the branched-chain aminotransferase from S. mutans is reported at 1.9 Å resolution.

A universal indicator dye pH assay for crystallization solutions and other high-throughput applications

A rapid plate-based pH assay has been developed that takes advantage of the automation available in a protein-crystallization laboratory.

Proline: Mother Nature's cryoprotectant applied to protein crystallography

The amino acid L-proline is shown to be a good cryoprotectant for protein crystals. Four examples are provided; the range of proline used for cryoprotection is 2.0–3.0 M.

Structural and biochemical characterization of a trapped coenzyme A adduct of Caenorhabditis elegans glucosamine-6-phosphate N-acetyltransferase 1

Glucosamine-6-phosphate N-acetyltransferase is an essential enzyme of the eukaryotic UDP-GlcNAc biosynthetic pathway. A crystal structure at 1.55 Å resolution revealed a highly unusual covalent product complex and biochemical studies investigated the function of a fully conserved active-site cysteine.

The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein

The promiscuous binding of an NS5A peptide to the Fyn SH3 domain is described.

X-ray structure of p38α bound to TAK-715: comparison with three classic inhibitors

The first X-ray structure of p38α cocrystallized with TAK-715 is presented, as well as new high-resolution structures of p38α bound to SB-203580, SCIO-469 and VX-745. The impact of crystallization conditions and selectivity profiles on protein conformation is discussed.

High-resolution crystal structure of the isolated ribosomal L1 stalk

The crystal structure of the isolated full-length ribosomal L1 stalk has been solved at high resolution, detailed analysis of L1-rRNA interactions and crystal packing has been carried out.

Dimerization properties of the RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesis

Crystallization of RpBphP2-CBD was achieved by homologue-directed mutagenesis via dimer formation in solution by the mutation N136R. Naturally occurring mutations in BphPs correlate well with their observed dimerization properties and suggests a structural diversity within this family.

Continuous β-turn fold of an alternating alanyl/homoalanyl peptide nucleic acid

The 1.0 Å crystal structure of an alternating L-homoalanyl, D-alanyl peptide nucleic acid reveals a novel tetrameric cage with Watson–Crick pairing of the stacked nucleobases.