The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft

The structure of a xylanase from F. oxysporum (FoXyn10a) was determined at 1.94 Å resolution. FoXyn10a adopts the (β/α)₈-barrel fold of the GH10 family, with an extended loop above the catalytic site with potential implications for enzymatic function.

Structural basis of nuclear import of flap endonuclease 1 (FEN1)

The crystal structure of the complex between the nuclear transport factor importin-α and the peptide corresponding to the nuclear localization sequence from flap 1 endonuclease (FEN1) has been determined. The structure rectifies the binding mode previously proposed and therefore explains the functional results that were previously controversial.

Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus

Succinyl-CoA synthetase catalyzes the reaction succinyl-CoA + NDP + P_i ⇌ succinate + CoA + NTP, where N denotes adenosine or guanosine. The enzyme from T. aquaticus was characterized biochemically and its structure was determined in complex with GDP-Mn²⁺, the preferred nucleotide.

Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus

X-ray structures of S. solfataricus serine:pyruvate aminotransferase in different intermediate states and in complex with inhibitor have increased our understanding of the enzyme mechanism and have allowed an insight into the substrate specificity of this industrially important enzyme.

Structures of Helicobacter pylori uridylate kinase: insight into release of the product UDP

Two crystal structures of UMPK from Helicobacter pylori in complex with GTP and with UDP are reported.

Structures of Staphylococcus aureus peptide de­formylase in complex with two classes of new inhibitors

Crystal structures of peptide deformylase from S. aureus in complex with novel inhibitors are presented together with their functional analysis. A detailed comparative analysis of these structures as well as the activities of the inhibitors allowed the elucidation of distinctive structural changes which depend upon the class of inhibitor.

Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato

The structure of potato serine protease inhibitor, the most abundant protease inhibitor in potatoes, is reported and sheds light on the inhibition mechanism of this protein.

Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness

A bond-distance analysis to determine the protonation states of ionizable amino acids has been made for trypsin at 1.2 Å resolution, subtilisin at 1.26 Å resolution and lysozyme at 0.65 Å resolution. This was effective for Asp and Glu but not for His.

Outrunning free radicals in room-temperature macromolecular crystallography

A systematic increase in lifetime is observed in room-temperature protein and virus crystals through the use of reduced exposure times and a fast detector.

A single mutation reforms the binding activity of an adhesion-deficient family 3 carbohydrate-binding module

Crystal structures of the family 3b carbohydrate-binding module (CBM3b) of the cellulosomal multimodular hydrolytic enzyme cellobiohydrolase 9A (Cbh9A) from C. thermocellum and of its mutant Cbh9A CBM3b^N126W have been determined at 2.20 and 1.04 Å resolution, respectively. This mutation reforms the cellulose-binding properties of the adhesion-deficient CBM.

High-resolution structures of Neotermes koshunensis β-glucosidase mutants provide insights into the catalytic mechanism and the synthesis of glucoconjugates

The single mutation E193D of the catalytic acid/base of Neotermes koshunensis β-glucosidase makes it favour the transglycosylation reaction. The NkBgl E193D mutant may be suitable for development as a useful tool for the enzymatic synthesis of numerous therapeutic oligosaccharides.

ATP forms a stable complex with the essential histidine kinase WalK (YycG) domain

The histidine WalK (YycG) plays a crucial role in coordinating murein synthesis with cell division and the crystal structure of its ATP binding domain has been determined. Interestingly the bound ATP was not hydrolyzed during crystallization and remains intact in the crystal lattice.

The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding property

The crystal structure of a putative general stress protein from the citrus canker bacterium X. citri pv. citri was determined to 2.5 Å resolution.

Low- and room-temperature X-ray structures of protein kinase A ternary complexes shed new light on its activity

ATP bound in the active site of protein kinase A is readily hydrolysed to ADP and free phosphate by X-ray irradiation at room temperature. The phosphate ion observed in the active site causes a dramatic conformational change of the bound peptide inhibitor.

Improved crystallographic models through iterated local density-guided model deformation and reciprocal-space refinement

A density-based procedure is described for improving a homology model that is locally accurate but differs globally. The model is deformed to match the map and refined, yielding an improved starting point for density modification and further model-building.

Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes. Corrigendum

A correction is made to the article by Prabu et al. [(2008). Acta Cryst. D64, 1146–1157].

Macromolecular Crystallization and Crystal Perfection