Expression, purification, crystallization and crystallographic characterization of dimeric and monomeric human neutrophil gelatinase associated lipocalin (NGAL)
| Autor: | F. C. Wiberg, T. Bratt, J. B. Cowland, Niels Borregaard, A. J. Ewald, Roland K. Strong |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Stereochemistry
Neutrophils Dimer Tripeptide Lipocalin Crystallography X-Ray law.invention chemistry.chemical_compound Lattice constant Lipocalin-2 Structural Biology law Proto-Oncogene Proteins Gelatinase Humans Crystallization Oncogene Proteins Chemistry General Medicine Ligand (biochemistry) Lipocalins Crystallography Monomer Carrier Proteins Acute-Phase Proteins |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 54(Pt 1) |
| ISSN: | 0907-4449 |
| Popis: | Crystals of the monomeric and dimeric forms of human neutrophil gelatinase associated lipocalin have been grown in hanging-drop vapor-diffusion trials using PEG as a precipitating agent with recombinant protein expressed in a baculovirus-based system. Crystals of monomeric NGAL belong to the cubic space group P432 with lattice constants a = b = c = 126.6 Å; crystals of dimeric NGAL belong to the tetragonal space group P41212 (or its enantiomorph P43212) with lattice constants a = b = 54.14 and c = 121.56 Å. Isomorphous crystals of the NGAL dimer can be grown in the presence of ligand: the tripeptide N-formyl-Met-Leu-Phe. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text