1lgv: Difference between revisions

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[[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1lgv, resolution 1.95Å" />

'''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K'''<br />

==Overview==

Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary, by vapor diffusion under microgravity conditions in the 9 day US Space, Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large, (8 x 1.6 x 1.0 mm) crystal in a short time period is a strong endorsement, for the use of microgravity to produce crystals sufficiently large for, neutron diffraction studies. The Sea dimer crystallized in the, orthorhombic space group P2(1)2(1)2(1), with a = 48.9 A, b = 85.2 A, and c, = 114.0 A. The crystals grown in microgravity exhibited significantly, lower mosaicities than those of ground-based crystals and the X-ray, diffraction data had a lower overall B factor. Three-dimensional, structures determined by X-ray analysis at two temperatures (100 and 293, K) were indistinguishable from those obtained from ground-based crystals., However, both the crystallographic R factor and the free R factor were, slightly lower in the models derived from crystals produced in, microgravity. The major difference between the two crystal growth systems, is a lack of convection and sedimentation in a microgravity environment., This environment resulted in the growth of much larger, higher-quality, crystals of the Sea Bence-Jones protein. Structurally, heretofore, unrecognized grooves on the external surfaces of the Sea and other, immunoglobulin-derived fragments are regular features and may offer, supplementary binding regions for super antigens and other elongated, ligands in the bloodstream and perivascular tissues.

Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary by vapor diffusion under microgravity conditions in the 9 day US Space Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large (8 x 1.6 x 1.0 mm) crystal in a short time period is a strong endorsement for the use of microgravity to produce crystals sufficiently large for neutron diffraction studies. The Sea dimer crystallized in the orthorhombic space group P2(1)2(1)2(1), with a = 48.9 A, b = 85.2 A, and c = 114.0 A. The crystals grown in microgravity exhibited significantly lower mosaicities than those of ground-based crystals and the X-ray diffraction data had a lower overall B factor. Three-dimensional structures determined by X-ray analysis at two temperatures (100 and 293 K) were indistinguishable from those obtained from ground-based crystals. However, both the crystallographic R factor and the free R factor were slightly lower in the models derived from crystals produced in microgravity. The major difference between the two crystal growth systems is a lack of convection and sedimentation in a microgravity environment. This environment resulted in the growth of much larger, higher-quality crystals of the Sea Bence-Jones protein. Structurally, heretofore unrecognized grooves on the external surfaces of the Sea and other immunoglobulin-derived fragments are regular features and may offer supplementary binding regions for super antigens and other elongated ligands in the bloodstream and perivascular tissues.

==About this Structure==

1LGV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LGV OCA].

1LGV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LGV OCA].

==Reference==

Line 13:

[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Bourne, P.C.]]

[[Category: Bourne, P C.]]

[[Category: DeWitt, C.R.]]

[[Category: DeWitt, C R.]]

[[Category: Edmundson, A.B.]]

[[Category: Edmundson, A B.]]

[[Category: Ramsland, P.A.]]

[[Category: Ramsland, P A.]]

[[Category: Terzyan, S.S.]]

[[Category: Terzyan, S S.]]

[[Category: human bence-jones dimer]]

[[Category: induced fit]]

[[Category: microgravity crystallization]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lgv, resolution 1.95&Aring;" />
 '''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K'''<br />
 ==Overview==
-Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary, by vapor diffusion under microgravity conditions in the 9 day US Space, Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large, (8 x 1.6 x 1.0 mm) crystal in a short time period is a strong endorsement, for the use of microgravity to produce crystals sufficiently large for, neutron diffraction studies. The Sea dimer crystallized in the, orthorhombic space group P2(1)2(1)2(1), with a = 48.9 A, b = 85.2 A, and c, = 114.0 A. The crystals grown in microgravity exhibited significantly, lower mosaicities than those of ground-based crystals and the X-ray, diffraction data had a lower overall B factor. Three-dimensional, structures determined by X-ray analysis at two temperatures (100 and 293, K) were indistinguishable from those obtained from ground-based crystals., However, both the crystallographic R factor and the free R factor were, slightly lower in the models derived from crystals produced in, microgravity. The major difference between the two crystal growth systems, is a lack of convection and sedimentation in a microgravity environment., This environment resulted in the growth of much larger, higher-quality, crystals of the Sea Bence-Jones protein. Structurally, heretofore, unrecognized grooves on the external surfaces of the Sea and other, immunoglobulin-derived fragments are regular features and may offer, supplementary binding regions for super antigens and other elongated, ligands in the bloodstream and perivascular tissues.
+Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary by vapor diffusion under microgravity conditions in the 9 day US Space Shuttle Mission STS-95. In comparison to ground-based experiments, nucleation was facile and spontaneous in space. Appearance of a very large (8 x 1.6 x 1.0 mm) crystal in a short time period is a strong endorsement for the use of microgravity to produce crystals sufficiently large for neutron diffraction studies. The Sea dimer crystallized in the orthorhombic space group P2(1)2(1)2(1), with a = 48.9 A, b = 85.2 A, and c = 114.0 A. The crystals grown in microgravity exhibited significantly lower mosaicities than those of ground-based crystals and the X-ray diffraction data had a lower overall B factor. Three-dimensional structures determined by X-ray analysis at two temperatures (100 and 293 K) were indistinguishable from those obtained from ground-based crystals. However, both the crystallographic R factor and the free R factor were slightly lower in the models derived from crystals produced in microgravity. The major difference between the two crystal growth systems is a lack of convection and sedimentation in a microgravity environment. This environment resulted in the growth of much larger, higher-quality crystals of the Sea Bence-Jones protein. Structurally, heretofore unrecognized grooves on the external surfaces of the Sea and other immunoglobulin-derived fragments are regular features and may offer supplementary binding regions for super antigens and other elongated ligands in the bloodstream and perivascular tissues.
 ==About this Structure==
-LGV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LGV OCA].
+LGV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LGV OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Bourne, P.C.]]
+[[Category: Bourne, P C.]]
-[[Category: DeWitt, C.R.]]
+[[Category: DeWitt, C R.]]
-[[Category: Edmundson, A.B.]]
+[[Category: Edmundson, A B.]]
-[[Category: Ramsland, P.A.]]
+[[Category: Ramsland, P A.]]
-[[Category: Terzyan, S.S.]]
+[[Category: Terzyan, S S.]]
 [[Category: human bence-jones dimer]]
 [[Category: induced fit]]
 [[Category: microgravity crystallization]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:57:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:51 2008''