This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lgv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lgv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1lgv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lgv| PDB=1lgv | SCENE= }}
{{STRUCTURE_1lgv| PDB=1lgv | SCENE= }}
-
'''Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12720277}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12720277 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12720277}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Induced fit]]
[[Category: Induced fit]]
[[Category: Microgravity crystallization]]
[[Category: Microgravity crystallization]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:54:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:53:34 2008''

Revision as of 17:53, 2 July 2008

Template:STRUCTURE 1lgv

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

Template:ABSTRACT PUBMED 12720277

About this Structure

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 Wed Jul 2 20:53:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools