Expression, purification, crystallization and crystallographic characterization of dimeric and monomeric human neutrophil gelatinase associated lipocalin (NGAL)

R. K. Strong, T. Bratt, J. B. Cowland, N. Borregaard, F. C. Wiberg, A. J. Ewald

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)93-95
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number1
DOIs
StatePublished - Jan 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'Expression, purification, crystallization and crystallographic characterization of dimeric and monomeric human neutrophil gelatinase associated lipocalin (NGAL)'. Together they form a unique fingerprint.

Cite this