Open Access'MAD'ly phasing the extracellular domain of the LDL receptor: a medium‐sized protein, large tungsten clusters and multiple non‐isomorphous crystals
Author(s) -
Rudenko G.,
Henry L.,
Vonrhein C.,
Bricogne G.,
Deisenhofer J.
Publication year - 2003
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444903021383
Subject(s) - tungsten , extracellular , domain (mathematical analysis) , crystallography , phaser , chemistry , materials science , biophysics , physics , biochemistry , biology , mathematics , optics , metallurgy , mathematical analysis
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.