The first crystals and the 2.8 Å X-ray structure of full-length recombinant human butyrylcholinesterase are reported.

The structure of bovine pancreatic RNase A has been determined in complex with 2′-deoxyguanosine-5′-monophosphate (dGMP) at 1.33 Å resolution at room temperature in a previously unreported unit cell belonging to space group P3₁.

Esterase A4 (EA4) is a timer protein found in diapause eggs of the silkworm Bombyx mori. The gene for this metalloglycoprotein was cloned from B. mori eggs and expressed using a baculovirus expression system in silkworm pupae. Crystals of the purified protein have been grown that diffract to beyond 2.1 Å resolution at 100 K using synchrotron radiation.

Purification and crystallization of ginkbilobin-2 and its selenomethionine derivative allowed the collection of complete data to 2.38 Å resolution and multiwavelength anomalous diffraction data sets, respectively.

A water-soluble chlorophyll-binding protein with photoconvertibility from C. album was extracted, purified and crystallized in a darkroom. The crystal diffracted to around 2.0 Å resolution.

The modular choline-binding protein F (CbpF) from S. pneumoniae has been crystallized by the hanging-drop vapour-diffusion method. A SAD data set from a gadolinium-complex derivative has been collected to 2.1 Å resolution.

The novel bacterial nitroreductase YwrO from B. amyloliquefaciens has been crystallized in two different crystal forms. An initial molecular-replacement solution has been obtained using the mammalian NQO2 structure.

Preliminary X-ray analysis of the galacto-N-biose-/lacto-N-biose I-binding protein (GL-BP) of the ABC transporter from B. longum is described.

The crystallization and preliminary X-ray diffraction analysis of cellobiohydrolase from M. albomyces is reported.

A preliminary X-ray crystal structural study of a soluble cognate T-cell receptor (TCR) in complex with a pMHC presenting the Melan-A peptide (ELAGIGILTV) is reported. The TCR and pMHC were refolded, purified and mixed together to form complexes, which were crystallized using the sitting-drop vapour-diffusion method. Single TCR–pMHC complex crystals were cryocooled and used for data collection.

The expression, purification and crystallization of recombinant human mitochondrial phenylalanyl-tRNA synthetase (mitPheRS) are reported. Diffraction data were collected to 2.2 Å resolution and the mitPheRS structure was solved using the molecular-replacement method.

The [NiFe]-hydrogenase maturation protein HypE was purified and crystallized. Crystals of HypE suitable for data collection diffracted to 1.55 Å resolution.

Preliminary X-ray analysis of the proliferation-associated protein Ebp1 from Homo sapiens is provided.

Selenomethionine-substituted crystals of the cytosolic domain of the cation diffusion facilitator family protein from T. maritima diffracted X-rays to 2.5 Å and belonged to space group R32, with unit-cell parameters a = b = 97.7, c = 83.4 Å.

Dextran glucosidase from S. mutans was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.2 Å resolution.

A thermostable esterase (EstA) from Thermotoga maritima was cloned and purified. Crystals of EstA and its selenomethionine derivative were grown and diffract to beyond 2.6 Å resolution at 100 K using synchrotron radiation.

The purification, crystallization, X-ray diffraction data acquisition and molecular-replacement results of royal palm tree (R. regia) peroxidase are described.

An N-terminal fragment of S. cerevisiae Hsp104 has been crystallized. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.

Crystallization of important glycoenzymes involved in IgE-mediated latex allergy.

The putative fumarylacetoacetase TTHA0809 from T. thermophilus HB8 has been overexpressed, purified and crystallized. The crystals diffracted X-rays to 2.2 Å resolution using synchrotron radiation.

The crystallization of the small subunit of the heterodimeric restriction endonuclease R.BspD6I and diffraction data collection to 1.5 Å resolution are reported.

The C-terminal soluble domain of the catalytic subunit (STT3) of the oligosaccharyltransferase from P. furiosus was purified and crystallized. A native crystal and a SeMet derivative have been analyzed using X-ray diffraction.

Here, the expression, purification, crystallization and X-ray diffraction data of a family 3 β-glucosidase from the hyperthermophilic bacterium Thermotoga neapolitana are reported.

A potential target for antibiotic drug design, d-alanine-d-alanine ligase from S. mutans, was expressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution.

A glucosamine 6-phosphate deaminase homologue from S. mutans was expressed, purified and crystallized. Diffraction data have been collected to 2.4 Å resolution.

A novel Nudix hydrolase Orf141 from E. coli, which cleaves pyrimidine deoxynucleoside triphosphates, was recently cloned. In order to illuminate the structural and functional features of the novel Nudix hydrolase Orf141, it was expressed, purified and crystallized and a preliminary X-ray crystallographic analysis was conducted.

A heterodimeric complex consisting of the C-terminal domains of human nucleoporins Nup107 and Nup133 was purified and crystallized and complete diffraction data sets were collected.