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1lgv
From Proteopedia
(New page: 200px<br /><applet load="1lgv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lgv, resolution 1.95Å" /> '''Structure of a Human...) |
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| - | [[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size=" | + | [[Image:1lgv.jpg|left|200px]]<br /><applet load="1lgv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lgv, resolution 1.95Å" /> | caption="1lgv, resolution 1.95Å" /> | ||
'''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K'''<br /> | '''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystals of a human (Sea) Bence-Jones dimer were produced in a capillary | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bourne, P | + | [[Category: Bourne, P C.]] |
| - | [[Category: DeWitt, C | + | [[Category: DeWitt, C R.]] |
| - | [[Category: Edmundson, A | + | [[Category: Edmundson, A B.]] |
| - | [[Category: Ramsland, P | + | [[Category: Ramsland, P A.]] |
| - | [[Category: Terzyan, S | + | [[Category: Terzyan, S S.]] |
[[Category: human bence-jones dimer]] | [[Category: human bence-jones dimer]] | ||
[[Category: induced fit]] | [[Category: induced fit]] | ||
[[Category: microgravity crystallization]] | [[Category: microgravity crystallization]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:51 2008'' |
Revision as of 11:44, 21 February 2008
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Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K
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.
About this Structure
1LGV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Comparison of the three-dimensional structures of a human Bence-Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS-95., Terzyan SS, Bourne CR, Ramsland PA, Bourne PC, Edmundson AB, J Mol Recognit. 2003 Mar-Apr;16(2):83-90. PMID:12720277
Page seeded by OCA on Thu Feb 21 13:44:51 2008
