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PDBsum entry 1eb6
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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 quick solution: ab initio structure determination of a 19 kda metalloproteinase using acorn.
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Authors
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K.E.Mcauley,
Y.Jia-Xing,
E.J.Dodson,
J.Lehmbeck,
P.R.Østergaard,
K.S.Wilson.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1571-1578.
[DOI no: ]
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PubMed id
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Abstract
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A data set from the metalloproteinase deuterolysin was collected at atomic
resolution (1.0 A) with synchrotron radiation. The high resolution allowed the
structure to be solved with the new direct-methods program ACORN using the
coordinates of the Zn atom as a starting point. The phases obtained from ACORN
were of sufficient quality to allow automated building to be carried out in
ARP/wARP. Minimal manual rebuilding of the model was required and the structure
determination was completed using the maximum-likelihood refinement program
REFMAC. The whole process, starting from the processed and merged data and
ending with a refined model, required less than 6 h of computational time.
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Figure 1.
Figure 1 v = 0.5 Harker sections of (a) the anomalous difference
and (b) the sharpened native Patterson functions.
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Figure 5.
Figure 5 Comparison of the metalloproteinases (a) snapalysin
(PDB code [148]1kuh ), (b) astacin (PDB code [149]1iab ), (c)
deuterolysin, (d) leishmanolysin (PDB code [150]1lml ) and (e)
thermolysin (PDB code [151]2tmn ). The matching
secondary-structure elements are shown as either cylinders (for
helices) or arrows (for sheets) and the remainder of the protein
is shown as a smoothed C^ [152][alpha] trace.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1571-1578)
copyright 2001.
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