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PDBsum entry 1vkq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A redetermination of the structure of the triple mutant (k53,56,120m) of phospholipase a2 at 1.6 a resolution using sulfur-Sas at 1.54 a wavelength.
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Authors
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K.Sekar,
V.Rajakannan,
D.Velmurugan,
T.Yamane,
R.Thirumurugan,
M.Dauter,
Z.Dauter.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
1586-1590.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the triple mutant K53,56,120M of bovine pancreatic
phospholipase A(2) has been redetermined using sulfur single-wavelength
anomalous scattering. The synchrotron data were collected at lambda = 1.54 A and
the crystal diffracted to 1.6 A resolution. The program SOLVE was used to locate
the heavy atoms and to estimate the initial phases and the resulting map was
then subjected to RESOLVE. The output of 455 non-H atoms, including 12 S atoms,
one calcium ion and one chloride ion, were then subjected to ARP/wARP followed
by REFMAC. With the improved phases, the automatic model building successfully
built more than 85% of the 123 residues, excluding the N- and C-terminal
residues. The final crystallographic R factor is 17.7% (R(free) = 21.7%). The
refined model consists of 954 non-H protein atoms, 165 water O atoms, three
2-methyl-2,4-pentanediol (MPD) molecules, one calcium ion and one chloride ion.
The present work is yet another example that shows the utility of
single-wavelength anomalous scattering data for solving a protein structure.
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Figure 2.
Figure 2 A stereoview of the omit electron-density map showing
the chloride ion and its liganded atoms. Contours are shown at
1.2  .
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
1586-1590)
copyright 2004.
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