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PDBsum entry 2g4l
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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C.Mueller-Dieckmann,
S.Panjikar,
A.Schmidt,
S.Mueller,
J.Kuper,
A.Geerlof,
M.Wilmanns,
R.K.Singh,
P.A.Tucker,
M.S.Weiss.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2007,
63,
366-380.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1 Anomalous scattering length (  f'']
) values in units of electrons at  =
1.0 Å (red) and =
2.0 Å (green) for elements 11-20 according to Cromer &
Liberman (1970[Cromer, D. & Liberman, D. (1970). J. Chem. Phys.
53, 1891-1898.]).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
366-380)
copyright 2007.
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