'MAD'ly phasing the extracellular domain of the LDL receptor: a medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals.
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.
Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard Y 4-206, Dallas, Texas 75390, USA.
G
G
Rudenko
L
L
Henry
C
C
Vonrhein
G
G
Bricogne
J
J
Deisenhofer
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004583:Electrons; D007313:Insecta; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D011973:Receptors, LDL / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014414:Tungsten / Q000737:chemistry*
D008024:Ligands; D011973:Receptors, LDL; D014414:Tungsten