Biomedical subjects

P Reichert

Publications and source records attributed to P Reichert.

12 recordsLinked to original sources

PubMed1992

Crystal structure of recombinant human interleukin-4.

The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are arranged in a left-handed antiparallel bundle with two overhand connections. Within these connections is a two-stranded antiparallel beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are similar to those of human granulocyte-macrophage colony-stimulating factor. Critical regions for receptor binding are proposed.

Amino Acid Sequence↗

PubMed1991

Crystallization and preliminary X-ray investigation of recombinant human interleukin 4.

Crystals of recombinant human interleukin 4 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space-group P4(1)2(1)2 or P4(3)2(1)2; the unit cell axes are a = 92.2(1) A and c = 46.4(1) A. The crystals are stable to X-rays for at least three days and diffract beyond 2.8 A resolution. The crystals contain approximately 63% solvent, assuming there is one molecule in the asymmetric unit.

Humans↗

PubMed1991

252Cf-plasma desorption and cesium-ion liquid secondary-ion mass spectrometric analysis of recombinant proteins.

The 35 keV Cs+ liquid secondary-ion mass spectrometry (LSIMS) and 252Cf-plasma desorption (PD) mass spectra of recombinant proteins in the 10-25 kDa mass range are compared. Both techniques showed comparable mass accuracy and sensitivity, and in the case of LSIMS, remarkably short analysis time. Analysis by the PD/nitrocellulose method demonstrated slightly higher sensitivity and relatively lower dependence on the salt and buffer content of the protein sample.

Animals↗

PubMed1991

Utility of phenomenological models for describing temperature dependence of bacterial growth.

We compared three unstructured mathematical models, the master reaction, the square root, and the damage/repair models, for describing the relationship between temperature and the specific growth rates of bacteria. The models were evaluated on the basis of several criteria: applicability, ease of use, simple interpretation of model parameters, problem-free determination of model parameters, statistical evaluation of goodness of fit (chi 2 test), and biological relevance. Best-fit parameters for the master reaction model could be obtained by using two consecutive nonlinear least-square fits. The damage/repair model proved to be unsuited for the data sets considered and was judged markedly overparameterized. The square root model allowed nonproblematical parameter estimation by a nonlinear least-square procedure and, together with the master reaction model, was able to describe the temperature dependence of the specific growth rates of Klebsiella pneumoniae NCIB 418, Escherichia coli NC3, Bacillus sp. strain NCIB 12522, and the thermotolerant coccobacillus strain NA17. The square root and master reaction models were judged to be equally valid and superior to the damage/repair model, even though the square root model is devoid of a conceptual basis.

Bacteria↗

PubMed1990

Crystallization and preliminary x-ray investigation of recombinant human granulocyte-macrophage colony-stimulating factor.

Crystals of recombinant human granulocyte-macrophage colony-stimulating factor have been grown from solutions of polyethylene glycol 8000. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 45.5(1), b = 58.7(1) and c = 127.3(1) A. The crystals are stable to x-rays for at least 3 days and diffract beyond 2.8-A resolution. Although the molecule exists as a monomer in solution, it crystallizes with two or three molecules in the asymmetric unit.

Chemical Phenomena↗

PubMed1987

Crystallization and preliminary X-ray investigation of a recombinant form of human gamma-interferon.

A genetically engineered human gamma-interferon has been crystallized from solutions of ammonium sulfate. The crystals are trigonal, space group R32, with hexagonal axes of a = 114.0(1) A and c = 314.9(2) A. The crystals are moderately stable to x-rays and diffract to 2.85-A resolution. Density measurements indicate that the crystallographic asymmetric volume contains four interferon molecules.

Cloning, Molecular↗

PubMed1979