1lhz
From Proteopedia
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| - | [[Image:1lhz.gif|left|200px]] | + | [[Image:1lhz.gif|left|200px]] |
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| - | '''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 293K''' | + | {{Structure |
| + | |PDB= 1lhz |SIZE=350|CAPTION= <scene name='initialview01'>1lhz</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 293K''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LHZ is a [ | + | 1LHZ is a [[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=1LHZ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12720277 12720277] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: microgravity crystallization]] | [[Category: microgravity crystallization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:05 2008'' |
Revision as of 10:31, 20 March 2008
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Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 293K
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
1LHZ 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 Mar 20 12:31:05 2008
