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 language||English (US)|
|Number of pages||9|
|Journal||Acta Crystallographica - Section D Biological Crystallography|
|State||Published - Nov 2003|
ASJC Scopus subject areas
- Structural Biology