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Updated: Jul 24, 2026
Crystallization of Membrane Proteins in Lipidic Mesophases
Published on: March 28, 2011
'MAD'ly phasing the extracellular domain of the LDL receptor: a medium-sized protein, large tungsten clusters and
G Rudenko1, L Henry, C Vonrhein
1Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard Y 4-206, Dallas, Texas 75390, USA.
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 A) with multiple non-isomorphous crystals containing 31 W atoms in the asymmetric unit.
