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.
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Schedule a callMore From: Acta crystallographica. Section D, Biological crystallography
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