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PDBsum entry 1ld2
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DOI no:
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Acta Crystallogr D Biol Crystallogr
57:929-940
(2001)
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PubMed id:
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Structural effects of monovalent anions on polymorphic lysozyme crystals.
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M.C.Vaney,
I.Broutin,
P.Retailleau,
A.Douangamath,
S.Lafont,
C.Hamiaux,
T.Prangé,
A.Ducruix,
M.Riès-Kautt.
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ABSTRACT
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Understanding direct salt effects on protein crystal polymorphism is addressed
by comparing different crystal forms (triclinic, monoclinic, tetragonal and
orthorhombic) for hen, turkey, bob white quail and human lysozymes. Four new
structures of hen egg-white lysozyme are reported: crystals grown in the
presence of NapTS diffracted to 1.85 A, of NaI to 1.6 A, of NaNO(3) to 1.45 A
and of KSCN to 1.63 A. These new structures are compared with previously
published structures in order to draw a mapping of the surface of different
lysozymes interacting with monovalent anions, such as nitrate, chloride, iodide,
bromide and thiocyanate. An analysis of the structural sites of these anions in
the various lysozyme structures is presented. This study shows common anion
sites whatever the crystal form and the chemical nature of anions, while others
seem specific to a given geometry and a particular charge environment induced by
the crystal packing.
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Selected figure(s)
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Figure 4.
Figure 4 R.m.s. deviations versus the sequence number between
the two independent molecules of the HEWL/NaI monoclinic
structure showing the non-equivalence of loops 65-75.
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Figure 6.
Figure 6 All anionic sites (red numbers) aligned on the lysozyme
sequence. The unique sites are labelled according to the
chemical formula of the anion taken from the corresponding PDB
file.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
929-940)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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V.Babin,
C.Roland,
and
C.Sagui
(2011).
The α-sheet: A missing-in-action secondary structure?
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Proteins,
79,
937-946.
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Y.R.Gokarn,
R.M.Fesinmeyer,
A.Saluja,
V.Razinkov,
S.F.Chase,
T.M.Laue,
and
D.N.Brems
(2011).
Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions.
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Protein Sci,
20,
580-587.
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E.Pozharski
(2010).
Percentile-based spread: a more accurate way to compare crystallographic models.
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Acta Crystallogr D Biol Crystallogr,
66,
970-978.
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Y.Zhang,
and
P.S.Cremer
(2009).
The inverse and direct Hofmeister series for lysozyme.
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Proc Natl Acad Sci U S A,
106,
15249-15253.
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M.Benvenuti,
and
S.Mangani
(2007).
Crystallization of soluble proteins in vapor diffusion for x-ray crystallography.
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Nat Protoc,
2,
1633-1651.
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P.E.Mason,
G.W.Neilson,
C.E.Dempsey,
A.C.Barnes,
and
J.M.Cruickshank
(2003).
The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution.
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Proc Natl Acad Sci U S A,
100,
4557-4561.
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S.Majeed,
G.Ofek,
A.Belachew,
C.C.Huang,
T.Zhou,
and
P.D.Kwong
(2003).
Enhancing protein crystallization through precipitant synergy.
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Structure,
11,
1061-1070.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
