'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 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

Fingerprint

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

@article{c8c56b14933f4d86aabd1994b1a03efa,
title = "'MAD'ly phasing the extracellular domain of the LDL receptor: A medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals",
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 {\AA}) with multiple non-isomorphous crystals containing 31 W atoms in the asymmetric unit.",
author = "G. Rudenko and L. Henry and C. Vonrhein and G. Bricogne and J. Deisenhofer",
year = "2003",
month = "11",
doi = "10.1107/S0907444903021383",
language = "English (US)",
volume = "59",
pages = "1978--1986",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

TY - JOUR

T1 - 'MAD'ly phasing the extracellular domain of the LDL receptor

T2 - A medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals

AU - Rudenko, G.

AU - Henry, L.

AU - Vonrhein, C.

AU - Bricogne, G.

AU - Deisenhofer, J.

PY - 2003/11

Y1 - 2003/11

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0242713123&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242713123&partnerID=8YFLogxK

U2 - 10.1107/S0907444903021383

DO - 10.1107/S0907444903021383

M3 - Article

C2 - 14573953

AN - SCOPUS:0242713123

VL - 59

SP - 1978

EP - 1986

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 11

ER -