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.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
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.
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U2 - 10.1107/S0907444903021383
DO - 10.1107/S0907444903021383
M3 - Article
C2 - 14573953
AN - SCOPUS:0242713123
SN - 0907-4449
VL - 59
SP - 1978
EP - 1986
JO - Acta Crystallographica - Section D Biological Crystallography
JF - Acta Crystallographica - Section D Biological Crystallography
IS - 11
ER -