September 1996 issue
Cover illustration: NMR solution structure of an Antennapedia homeodomain complex with a 14-base pair operator DNA duplex. The dotted surface outlines a hydrated cavity in the protein-DNA interface.
Starting sets comprising of 26 single phases, or alternatively 45 triplet phases, assumed known from three-beam diffraction experiments were sufficient to initiate structure solution of rubredoxin by direct methods with data at 1.54 Å resolution.
Glutaraldehyde cross-linking has been used to study the aggregation of lysozyme in supersaturated solutions.
Molecular edges can be extracted in the averaged difference map by a Monte-Carlo method.
In the Mn, Cd and Tb metal complexes of troponin C, the metals again exhibit pentagonal bipyramidal coordination like Ca, except Mn at site 4 which exhibits an intermediate approaching the hexacoordinate Mg.
The human protective protein also known as protective protein/ cathepsin A is essential for humans as demonstrated by its deficiency, resulting in the lysosomal storage disease galactosialidosis. This paper describes the crystal structure determination which was unique in that twofold density averaging in combination with mask optimization procedures enabled 314 residues to be added to the 588 residues of the initial molecular replacement model.
The direct method has been shown to be capable of phasing anomalous scattering data collected at one wavelength from a native pattern.
The adenovirus ssDNA-binding protein shows conformational changes by altered crystal packing effected by soaking crystals in K3UO2F5 solutions.
A modified neurophysin, des 1-6 bovine neurophysin II, has been crystallized in space group P3121 (or P3221) with a = b = 48.9, c = 78.6 Å. These crystals represent the first crystals of ligand-free neurophysin and are essential for understanding hormone-induced neurophysin dimerization.
The structures and spectral properties of the copper-containing mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative have been studied.
The flash-freezing technique may lead to a modulated structure in a protein crystal. Such phenomena, when unnoticed, may lead to misinterpretation of results and false conclusions about crystal geometry and completeness of data.
The overall structures of Val122Ile mutant and wild-type trans-thyretin are essentially identical. However, there are small changes that seem to confirm a tendancy for a less stable tetrameric structure.
The statistical significance of molecular replacement solutions with NMR templates is enhanced if distance-derived B factors are used.
Determination of molecular growth mechanisms and surface morphology of tetragonal lysozyme crystals from a modified PBC theory and analyses of previous experiments.
The structure of the DNA octamer d(CCCTAGGG) has been determined and compared with nine other isomorphous sequences.
High-pressure crystallography on single crystals of proteins is being developed as a tool to investigate tertiary and quaternary structure changes. First results indicate that application of only moderate pressure promotes unit-cell changes in rhomohedral insulin.
Crystals of human salivary α-amylase inhibitor from wheat have been obtained. A native data set was collected at laboratory sources up to 2.1 Å resolution.
A 26-nucleotide RNA pseudoknot produces crystals that diffract to 2.9 Å resolution. The structure is being determined by MIR using bromo-uridine derivatives.
This paper reports the purification and successful crystallization of a mannose-specific lectin from bluebell bulbs. Data to 1.86 Å resolution have been recorded and the structure solved by the molecular replacement method.
Porcine heart mitochondrial NADP+-dependent isocitrate dehydrogenase has been crystallized from polyethylene glycol/ sodium sulfate mixtures in the presence of Mg2+ and isocitrate.
Two crystal forms of lysinal derivatives of Achromobacter protease I have been obtained. These crystals diffract around 2 Å resolution and are suitable for crystal structure determination.
It was found that 3-isopropylmalate dehydrogenase from Bacillus coagulans crystallizes in three crystallline forms and that the trigonal form, which has an unusually high solvent content, is suitable for X-ray analysis.
This paper presents the purification, crystallization and preliminary analysis of the Ras binding domain of RalGDS, a guanine nucleotide dissociation stimulator of the Ral protein, in its native form and in its selenomethinonie derivative form. The native crystals diffract to 1.8 Å at a synchrotron radiation source.
A bifunctional enzyme, OPET decarboxylase/HHDD isomerase has been crystallized using PEG as a precipitant. The structure determination is underway using MIR methods.
Human dUTPase has been crystallized. Crystals belong to the space group P212121 with one trimer of identical subunits in the assymetric unit.
The haemagglutinin-esterase fusion glycoprotein of influenza C virus has been crystallized. Data have been collected from two tetragonal crystal forms using synchrotron radiation and flash-cooling techniques.
Crystals of isoform I of the lectin from C. mollis have been grown from PEG 6000 as a precipitant by the hanging-drop technique. Two forms were obtained belonging to space groups I222 and P212121.