Apo and GDP-bound crystal structures of an essential GTPase, YsxC, from T. maritima were determined to maximal resolutions of 2.3 and 1.9 Å, respectively. Switch I in GDP–YsxC can adopt both an `open' and `closed' conformation, suggesting a mechanism for diffusion of GDP out of the nucleotide-binding pocket.
The structure of a recombinant form of the sweet-tasting protein thaumatin I was determined at 1.1 Å resolution and refined to an Rwork of 9.1% and an Rfree of 11.7%. Comparisons with plant thaumatin revealed the electron density of recombinant thaumatin I to be significantly improved, especially around Asn46 and Ser63.
In this study, the catalytic subunit of E. coli AHAS II was cocrystallized with its cofactors Mg2+, FAD and ThDP using the sitting-drop vapour-diffusion method and the crystals diffracted to 2.80 Å resolution.
The P3 dimerization domain of CheA from E. coli has been crystallized (space group P1, unit-cell parameters a = 59.271, b = 67.674, c = 82.815 Å, α = 77.568, β = 86.073, γ = 64.436°). Diffraction data to 2.80 Å resolution have been collected using synchrotron radiation.
A recombinant form of geraniol dehydrogenase from Backhousia citriodora has been overexpressed in Escherichia coli and purified and crystallized by the sitting-drop method using polyethylene glycol 3350 as a precipitant.
The L. monocytogenes Ca2+-ATPase LMCA1 was crystallized in a Ca2+-free E2–AlF4− form. A complete data set extending to 4.3 Å resolution was collected and a molecular-replacement solution was obtained using sarcoplasmic reticulum Ca2+-ATPase as a search model.
The cloning, expression, purification, crystallization and preliminary X-ray analysis of a ferric binding protein encoded by T. thermophilus HB8 in apo and iron-bound holo states are presented. Four different crystal forms were obtained.
An O-methyltransferase from the ubiquinone-biosynthesis pathway in Escherichia coli, UbiG, with an N-terminal hexahistidine tag has been expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.00 Å resolution.
The eukaryotic translation initiation factor eIF5BΔN and the eIF5BΔN–eIF1AΔN complex from S. cerevisiae were crystallized. The crystals diffracted to maximum resolutions of 2.45 and 3.3 Å, respectively.