'MAD'ly phasing the extracellular domain of the LDL receptor: A medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals

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

Research output: Contribution to journalArticle

18 Scopus citations

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 1 2003

ASJC Scopus subject areas

  • Structural Biology

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