2ILL

Anomalous substructure of Titin-A168169

Summary for 2ILL

• Entry DOI: 10.2210/pdb2ill/pdb
• Descriptor: Titin, CHLORIDE ION (3 entities in total)
• Functional Keywords: long wavelength, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (Probable): Q8WZ42
• Total number of polymer chains: 1
• Total formula weight: 21708.60

Authors

Mueller-Dieckmann, C.,Weiss, M.S. (deposition date: 2006-10-03, release date: 2007-02-20, Last modification date: 2024-03-13)

Primary citation

Mueller-Dieckmann, C.,Panjikar, S.,Schmidt, A.,Mueller, S.,Kuper, J.,Geerlof, A.,Wilmanns, M.,Singh, R.K.,Tucker, P.A.,Weiss, M.S.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths
ACTA CRYSTALLOGR.,SECT.D, 63:366-380, 2007

PubMed Abstract: 23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.

PubMed: 17327674
DOI: 10.1107/S0907444906055624

Experimental method

X-RAY DIFFRACTION (2.2 Å)