1OBQ

Apocrustacyanin C1 crystals grown in space and earth using vapour diffusion geometry

Summary for 1OBQ

• Entry DOI: 10.2210/pdb1obq/pdb
• Related: 1GKA 1H91 1I4U 1OBU
• Descriptor: CRUSTACYANIN C1 SUBUNIT (2 entities in total)
• Functional Keywords: transport protein, lipocalin, antiparallel beta-strands, pigment
• Biological source: HOMARUS GAMMARUS (EUROPEAN LOBSTER)
• Cellular location: Secreted, extracellular space: P80029
• Total number of polymer chains: 2
• Total formula weight: 41376.12

Authors

Habash, J.,Boggon, T.J.,Raftery, J.,Chayen, N.E.,Zagalsky, P.F.,Helliwell, J.R. (deposition date: 2003-01-31, release date: 2003-07-03, Last modification date: 2011-07-13)

Primary citation

Habash, J.,Boggon, T.J.,Raftery, J.,Chayen, N.E.,Zagalsky, P.F.,Helliwell, J.R.
Apocrustacyanin C(1) Crystals Grown in Space and on Earth Using Vapour-Diffusion Geometry: Protein Structure Refinements and Electron-Density Map Comparisons
Acta Crystallogr.,Sect.D, 59:1117-, 2003

PubMed Abstract: Models of apocrustacyanin C(1) were refined against X-ray data recorded on Bending Magnet 14 at the ESRF to resolutions of 1.85 and 2 A from a space-grown and an earth-grown crystal, respectively, both using vapour-diffusion crystal-growth geometry. The space crystals were grown in the APCF on the NASA Space Shuttle. The microgravity crystal growth showed a cyclic nature attributed to Marangoni convection, thus reducing the benefits of the microgravity environment, as reported previously [Chayen et al. (1996), Q. Rev. Biophys. 29, 227-278]. A subsequent mosaicity evaluation, also reported previously, showed only a partial improvement in the space-grown crystals over the earth-grown crystals [Snell et al. (1997), Acta Cryst. D53, 231-239], contrary to the case for lysozyme crystals grown in space with liquid-liquid diffusion, i.e. without any major motion during growth [Snell et al. (1995), Acta Cryst. D52, 1099-1102]. In this paper, apocrustacyanin C(1) electron-density maps from the two refined models are now compared. It is concluded that the electron-density maps of the protein and the bound waters are found to be better overall for the structures of apocrustacyanin C(1) studied from the space-grown crystal compared with those from the earth-grown crystal, even though both crystals were grown using vapour-diffusion crystal-growth geometry. The improved residues are on the surface of the protein, with two involved in or nearby crystal lattice-forming interactions, thus linking an improved crystal-growth mechanism to the molecular level. The structural comparison procedures developed should themselves be valuable for evaluating crystal-growth procedures in the future.

PubMed: 12832753
DOI: 10.1107/S0907444903007959

Experimental method

X-RAY DIFFRACTION (1.85 Å)