An evaluation of the use of databases in protein structure refinement

Comparison of different X-ray refinement procedures suggests that the inclusion of information about known main- and side-chain conformations gives improved results

X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules

The structure of monoclinic hen egg-white lysozyme crystallized at 313 K was determined at 1.72 Å resolution. The conformations of the two independent molecules differ in the regions of residues 45-50, 65-73 and 100-104.

Solid-state phase transition in the crystal structure of ribulose 1,5-bis­phosphate carboxylase/oxygenase

When RuBisCO crystals are transferred from a high-salt low-pH mother liquor to conditions of low salt and high pH, they contract 24 Å along the c axis and shrink 14% in volume. Changes in the protein structure are relatively small.

Metal substitution in a blue-copper protein: the crystal structure of cadmium-azurin at 1.8 Å resolution

A high-resolution structure analysis of the protein azurin, with cadmium substituted for the native copper, shows that the overall structure is unchanged except for minor alterations to the metal coordination.

Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c₂ from Rhodopseudomonas viridis

The crystal structure of cytochrome c from Rhodopseudomonas viridis has been solved by an automatic molecular-replacement procedure and refined to an R value of 0.219 for diffraction data at 3 Å resolution.

Data collection at short wavelengths in protein crystallography

Protein crystallographic data, collected using 0.92 and 0.55 Å X-rays, are compared. No significant differences in data quality or signal-to-background ratio were found.

1.70 Å resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix

The structure displays the familiar myoglobin fold; however, the D helix is replaced by a well ordered random coil. This feature may be correlated with observed dioxygen affinity and dissociation.

High-resolution crystals and preliminary X-ray diffraction studies of a catalytic RNA

High-resolution single crystals of a catalytic RNA molecule have been obtained. The space group is P1 and the crystals diffract to a resolution of 2.4 Å.

Phase diagram and dilution experiments in the crystallization of carboxypeptidase G₂

A new method for uncoupling nucleation and growth, and therefore growing protein crystals in the advantageous metastable zone of the phase diagram, is described. It consists of diluting microbatch crystallization droplets directly, some time after their setup.

Low-resolution X-ray diffraction data obtained from hexagonal crystals of methylamine-treated α₂-macroglobulin

α-Macroglobulin is a protease scavenger found in blood plasma which entraps 1-2 protease molecules for later removal from blood by receptor-mediated endocytosis in the liver. Data to a resolution of 10 Å have been obtained using synchrotron radiation at cryogenic temperature.

Structure of copper- and oxalate-substituted human lactoferrin at 2.0 Å resolution

A high-resolution crystal structure analysis of copper- and oxalate-substituted human lactoferrin has shown how the protein accommodates different bound cations and anions by small internal adjustments.

Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 Å resolution

The crystal structure of pseudoazurin from Methylobacterium extorquens AM1 has been solved by the molecular replacement method and refined at 1.5 Å resolution.

Crystallization and preliminary crystallographic analysis of galactose-1-phosphate uridylyltransferase from Escherichia coli

Galactose-1-phosphate uridylyltransferase, an enzyme critical in sugar metabolism, has been crystallized. Preliminary crystallographic results are presented as well as methods of protein purification and crystallization.

A novel platinum reagent [chloro(2,2':6',2''-terpyridine)platinum(II) chloride] for use in heavy-atom derivatization of protein crystals

A platinum chromophore proves to be a useful reagent in heavy-atom derivatization of protein crystals.

Crystallization at low salt concentration and alkaline pH and preliminary crystallographic data for a monoclinic form of yeast enolase

Low-salt crystals are more suitable for ligand-binding studies, and thus investigations of the catalytic mechanism.