'MAD'ly phasing the extracellular domain of the LDL receptor

A medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals

Gabrielle Rudenko, L. Henry, C. Vonrhein, G. Bricogne, J. Deisenhofer

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The crystal structure of the extracellular domain of the LDL receptor (LDL-R) was determined in a MAD experiment using 12-tungstophosphate clusters as anomalous scatterers. While useful for phasing, the tungsten clusters rendered the crystals radiation-sensitive and non-isomorphous and profoundly altered the diffraction data, causing complications. The work is presented as a case study for phasing a medium-sized protein (700 residues) at low resolution (4 Å) with multiple non-isomorphous crystals containing 31 W atoms in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)1978-1986
Number of pages9
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number11
DOIs
StatePublished - Nov 2003
Externally publishedYes

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Tungsten
LDL Receptors
tungsten
Radiation
proteins
Crystals
crystals
Proteins
Diffraction
Crystal structure
Atoms
crystal structure
radiation
scattering
diffraction
atoms
Experiments
mycophenolic adenine dinucleotide

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

'MAD'ly phasing the extracellular domain of the LDL receptor : A medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals. / Rudenko, Gabrielle; Henry, L.; Vonrhein, C.; Bricogne, G.; Deisenhofer, J.

In: Acta Crystallographica - Section D Biological Crystallography, Vol. 59, No. 11, 11.2003, p. 1978-1986.

Research output: Contribution to journalArticle

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