Coordinate-based cluster analysis

This paper exploits the power of certain 4 x 4 matrices to show how cluster pairs may be selected from an ensemble of clusters of structures and united by superposition, thus developing a tree of related structures, such that each union so formed is the most compact available, All residuals and orientations are available at every stage, and coordinate transformations and average structures are not involved.

Do C—H^⋯O hydrogen bonds contribute to the stability of nucleic acid base pairs?

A geometric analysis suggests that in certain nucleic acid structures C-H⋯O hydrogen-bonding interactions may occur. These interactions could stabilize the base-base associations.

A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement

It was shown that the hexameric structure of an enzyme-inhibitor complex can be determined by molecular replacement using the structure of monomeric native protein as a probe molecule.

The three-dimensional structure of the aspartate receptor from Escherichia coli

The crystal structure of the ligand-binding domain of the Escherichia coli aspartate receptor was determined and compared to the analogous structures from Salmonella typhimurium.

Structure of the ferredoxin from Clostridium acidurici: model at 1.8 Å resolution

The crystal structure of a two iron-sulfur cluster protein the ferredoxin from Clostridium acidurici, has been solved from diffraction data up to 1.8 Å resolution. The refinement was performed by a molecular dynamic technique using the variable force constants.

Deconvolution of fully overlapped reflections from crystals of foot-and-mouth disease virus O₁ G67

A simple procedure for obtaining interpretable electron-density maps for crystals where every reflection is exactly overlapped by one other, is presented. The method uses the redundancy inherent in a system possessing noncrystallographic symmetry to provide constraints enabling deconvolution of the data.

Structure of the azurin mutant Phe114Ala from Pseudomonas aeruginosa at 2.6 Å resolution

The crystal structure of azurin mutant Phe114Ala from P. aeruginosa has been solved to a final crystallographic R value of 18.5% to 2.6 Å resolution. The mutation was performed at residue Phe114 to investigate its suggested role in the electron self-exchange reaction.

Crystal structure of narbonin at 1.8 Å resolution

The structure of narbonin, a seed globulin with (α/β)₈-topology, has been refined using the cDNA sequence and compared with the X-ray sequence which was reported earlier. The classification of narbonin as a storage protein without enzymatic function is discussed.

X-ray structures of the B-DNA dodecamer d(CGCGTTAACGCG) with an inverted central tetranucleotide and its netropsin complex

Netropsin binding to the B-DNA dodecamer d(CGCGTTAACGCG) causes very little structural perturbation in the DNA.

Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16

The structure of a new alkaline serine protease, M-protease, was determined by molecular replacement using the coordinates of subtilisin Carlsberg, and refined to a crystallographic R factor of 0.189 at 2.4 Å resolution.

Growth process of protein crystals revealed by laser Michelson interferometry investigation

Large single crystals of hen egg-white lysozyme and the determination of the temperature-dependence of their solubility allowed a new method to be used for the basic physicochemical understanding of the growth processes of protein crystals.

Crystallographic analysis of Phe→Leu substitution in the hydrophobic core of barnase

The crystal structure of a Phe→Leu mutation in the hydrophobic core of barnase reveals that the overall structural changes are minimal and that the side-chain conformation of the mutated residue is determined by conformational energy as well as the amount of hydrophobic surface area that is buried by that residue.

Cytochrome c₆ from the green alga Monoraphidium braunii. Crystallization and preminary diffraction studies

Preliminary crystal analysis of cytochrome c6, an electron carrier between chlorophyl molecule P700 of PSI and cytochrome f from the b_6f complex.

A new crystal form of bovine heart ubiquinol: cytochrome c oxidoreductase: determination of space group and unit-cell parameters

Bovine ubiquinol cytochrome c oxidoreductase has been crystallized in a new form. The space group is C222₁ with unit-cell parameters a = 384, b = 118 and c = 177 Å.

Crystallization of the NAD(P)-dependent glutamate de­hydrogenase from the hyperthermophile Pyrococcus furiosus

The NAD(P)-dependent GDH from the hyperthermophile P. furiosus has been crystallized by the hanging-drop method of vapour diffusion using lithium sulfate as a precipitant. The determination of the structure of this enzyme will be important in advancing our understanding of how proteins are adapted to enable them to survive at such extreme temperatures.

Crystallization and preliminary X-ray structure solution of Rhizomucor miehei aspartic proteinase

Single crystals of NAD-dependent GAPDH from E. coli have been obtained. They belonged to space group C222₁ with cell dimensions a = 79.1, b = 189.6 and c = 122.2 Å.

Crystallization and preliminary X-ray diffraction studies of Escherichia coli glyceraldehyde-3-phosphate de­hydrogenase

Single crystals of NAD-dependent GAPDH from E. coli have been obtained. They belonged to space group C222₁ with cell dimensions a = 79.1, b = 189.6 and c = 122.2 Å.

Principles of protein X-ray crystallography by J. Drenth