1LHZ

Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 293K

Summary for 1LHZ

• Entry DOI: 10.2210/pdb1lhz/pdb
• Related: 1JVK 1LGV
• Descriptor: IMMUNOGLOBULIN LAMBDA LIGHT CHAIN (2 entities in total)
• Functional Keywords: human bence-jones dimer, microgravity crystallization, induced fit, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 45217.96

Authors

Terzyan, S.S.,DeWitt, C.R.,Ramsland, P.A.,Bourne, P.C.,Edmundson, A.B. (deposition date: 2002-04-17, release date: 2003-07-01, Last modification date: 2023-08-16)

Primary citation

Terzyan, S.S.,DeWitt, C.R.,Ramsland, P.A.,Bourne, P.C.,Edmundson, A.B.
Comparison of the three-dimensional structures of a human Bence-Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS-95
J.MOL.RECOG., 16:83-90, 2003

PubMed Abstract: 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.

PubMed: 12720277
DOI: 10.1002/jmr.610

Experimental method

X-RAY DIFFRACTION (2.3 Å)