The future of crystallization communications in Acta Cryst. F

Editorial.

Crystallization reports are the backbone of Acta Cryst. F, but do they have any spine?

All the crystallization communications published in Acta Cryst. F in 2012 were analysed. Details of the analysis are presented, along with some suggestions for making this type of publication more useful.

Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii

The crystal structure of the archaeal peroxiredoxin from P. horikoshii was determined at a resolution of 2.25 Å and compared with that of a homologous protein from A. pernix.

The structure of the TOG-like domain of Drosophila melanogaster Mast/Orbit

The crystal structure of Mast-M1 has been determined at 2.0 Å resolution and provides the first detailed structural description of a TOG-like domain.

Structure of Escherichia coli AdhP (ethanol-inducible de­hydrogenase) with bound NAD

The crystal structure of E. coli AdhP (ethanol-inducible dehydrogenase) in complex with NAD is reported.

Structure of a family 3a carbohydrate-binding module from the cellulosomal scaffoldin CipA of Clostridium thermocellum with flanking linkers: implications for cellulosome structure

The structure of the cellulose-binding module of the C. thermocellum cellulosome-integrating protein A scaffoldin with portions of the C- and N-terminal flanking linker regions has been determined at 1.98 Å resolution.

Structures of MauG in complex with quinol and quinone MADH

Crystal structures of MauG in complexes with MADH with its TTQ cofactor in the quinone and quinol forms are reported.

High-resolution structure of the Tiam1 PH_n-CC-Ex domain

The structures of two Tiam1 PH_n-CC-Ex domain variants have been determined to resolutions of 1.98 and 2.15 Å. Biochemical data indicate that this domain binds the coiled-coil domain of Par3b. SAXS data are in excellent agreement with the structures, indicating that the solution and crystal structures are very similar.

Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3

Comparisons between polymorphic structures in space groups P1, P2₁2₁2₁ and P4₃2₁2 highlight the conformational stability of tetrameric CAT-3 and reveal a distortion in the tetrameric structure that has not previously been described.

Purification, crystallization and preliminary X-ray crystallographic study of the tRNA pseudouridine synthase TruB from Streptococcus pneumoniae

The RNA pseudouridine synthase TruB catalyses the isomerization of uridine to pseudouridine at residue 55 of elongator tRNAs. Here, the expression, purification, crystallization and preliminary crystallographic analysis of TruB from Streptococcus pneumoniae are reported.

Protein expression, crystallization and preliminary X-ray crystallographic analysis of the isolated Shigella flexneri VapC toxin

The purification and crystallization of the isolated toxin VapC (MvpT) from the VapBC toxin–antitoxin complex of the pathogen S. flexneri are reported. The crystals belonged to space group H3 and diffracted to 1.9 Å resolution.

Crystallization and X-ray diffraction analysis of the N-terminal domain of the Toll-like receptor signalling adaptor protein TRIF/TICAM-1

This report describes the crystallization and X-ray diffraction analysis of a regulatory domain of the Toll-like receptor signalling adaptor TRIF/TICAM-1 and its SeMet-labelled mutant containing two additional Met residues. This domain is unrelated in sequence to any protein of known structure.

Expression, derivatization, crystallization and experimental phasing of an extracellular segment of the human Robo1 receptor

Robo receptors participate in the orchestration of several developmental responses, most notably axonal guidance in the central nervous system (CNS). Here, the expression, derivatization, crystallization, and experimental phasing of the extracellular juxtamembrane segment of the human Robo1 receptor are described.

Crystallization and preliminary X-ray diffraction analysis of a thermostable GDSL-family esterase, EstL5, from Geobacillus thermodenitrificans T2

As a thermostable esterase with cold adaptation, EstL5 might be of significant industrial interest and value in scientific research. In order to provide new insights into the structure–function relationship of EstL5 and to help better understand the biochemical data, a project to determine the three-dimensional structure of this enzyme was initiated.

The mannose-specific lectin domains of Flo1p from Saccharomyces cerevisiae and Lg-Flo1p from S. pastorianus: crystallization and preliminary X-ray diffraction analysis of the adhesin–carbohydrate complexes

The N-terminal carbohydrate-binding domains of Flo1p and Lg-Flo1p from two different Saccharomyces spp. were overexpressed in E. coli, purified and crystallized in different conditions. A preliminary X-ray analysis of the crystallized flocculin–protein complexes is reported in this work.

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human histidine triad nucleotide-binding protein 2 (hHINT2)

Human histidine triad nucleotide-binding protein 2 (hHINT2) was cloned, expressed in E. coli, purified and crystallized. The initially obtained crystals of hHINT2 were used for a diffraction experiment and data were collected to 2.83 Å resolution.

Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the kinase domain of AtMAP4Kalpha2 from Arabidopsis thaliana

The kinase domain of AtMAP4Kalpha2 was cloned, expressed, purified and crystallized. The crystals diffracted to 1.9 Å resolution and belonged to space group C222₁, with unit-cell parameters a = 55.27, b = 82.93, c = 133.15 Å.

Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus

The GRASP65 GRASP domain from R. norvegicus has been expressed, purified and crystallized. The crystals belonged to space group P2₁2₁2, with unit-cell parameters a = 44.99, b = 104.29, c = 37.93 Å, and diffracted to 2.0 Å resolution.

X-ray diffraction studies on merohedrally twinned Δ1–62NtNBCe1-A crystals of the sodium/bicarbonate cotransporter

A truncated mutant missing the first 62 residues of the N-terminal, cytoplasmic domain of the sodium-bicarbonate NBCe1-A cotransporter crystallizes in space group P3₁ with pseudo-P3₁21 symmetry and a hemihedral twin fraction of 33.0%. Twinned fractions and twin-pair statistics over binned resolutions confirm that the calculated twin fraction is associated with hemihedral twinning and not to non-crystallographic symmetry.

Purification, crystallization and preliminary X-ray analysis of the AAA⁺ σ⁵⁴ activator domain of FlrC from Vibrio cholerae

The AAA⁺ σ⁵⁴ interaction domain of FlrC from V. cholerae has been cloned, overexpressed, purified and crystallized in a heptameric form. Crystals belonging to space group P2₁2₁2₁ produced diffraction data to 2.8 Å resolution.

Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies

The N-terminal PDZ-like domain of the human peripheral nervous system myelin protein periaxin has been crystallized and preliminary diffraction data are reported. The periaxin crystals diffracted X-rays to 2.85 Å resolution using synchrotron radiation.

Expression, crystallization and preliminary X-ray analysis of rice L-galactose de­hydrogenase

Rice L-galactose dehydrogenase was crystallized and X-ray diffraction data were collected to 1.2 Å resolution.

Crystallization and preliminary X-ray study of the deaminase AmnE from Pseudomonas sp. AP-3

The deaminase AmnE from Pseudomonas sp. AP-3 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for this recombinant enzyme.

Mimer: an automated spreadsheet-based crystallization screening system

An automated spreadsheet-based solution for macromolecular crystallization screening is presented that allows easy formulation and optimization of crystal screens via multiple approaches, including incomplete-factorial and grid screening.

A strategy for selecting the pH of protein solutions to enhance crystallization

The pH of a solution is an important parameter in crystallization that needs to be controlled in order to ensure success. In this study, the effects of the buffer and protein solution pH values on the results of screening are systematically investigated.