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Plant protein
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PDB id
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1ly0
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasmic vesicle
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2 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
58:2060-2065
(2002)
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PubMed id:
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Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.
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C.Charron,
A.Kadri,
M.C.Robert,
R.Giegé,
B.Lorber.
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ABSTRACT
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The intensely sweet protein thaumatin has been crystallized at 293 K in the
presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data
collection at 100 K. A comparison of the three-dimensional structure model
derived from a crystal grown in the presence of glycerol with that of a control
deprived of this additive reveals only minor changes in the overall structure
but a approximately 20% reduction in the number of water molecules. X-ray
topography analyses show that the overall quality of the crystals prepared in
the presence of this cryoprotectant is enhanced.
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Selected figure(s)
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Figure 2.
Figure 2 X-ray topographs of thaumatin crystals prepared in the
absence or presence of 15%(v/v) glycerol. The topographs were
taken at the angular position corresponding to the maximum
intensity of the (00l) reflection profiles. The dotted line is a
trace of the reflector planes and g is the diffraction vector.
(a) One of the best crystals that was grown so far in agarose
gel under microgravity (FWHM = 10''); (b) a crystal grown on
earth in solution under similar conditions but with 15%(v/v)
glycerol (FWHM = 6.5'').
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2002,
58,
2060-2065)
copyright 2002.
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Figure was
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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F.Capuano,
L.Paduano,
G.D'Errico,
G.Mangiapia,
and
R.Sartorio
(2011).
Diffusion in ternary aqueous systems containing human serum albumin and precipitants of different classes.
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Phys Chem Chem Phys, 13,
3319-3327.
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G.Pompidor,
O.Maury,
J.Vicat,
and
R.Kahn
(2010).
A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction.
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Acta Crystallogr D Biol Crystallogr, 66,
762-769.
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PDB code:
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M.Warkentin,
and
R.E.Thorne
(2010).
Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.
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Acta Crystallogr D Biol Crystallogr, 66,
1092-1100.
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J.Xu,
Y.Xue,
and
N.R.Skrynnikov
(2009).
Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent.
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J Biomol NMR, 45,
57-72.
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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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B.Kauffmann,
M.S.Weiss,
V.S.Lamzin,
and
A.Schmidt
(2006).
How to avoid premature decay of your macromolecular crystal: a quick soak for long life.
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Structure, 14,
1099-1105.
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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
