1OBQ
Apocrustacyanin C1 crystals grown in space and earth using vapour diffusion geometry
1OBQ の概要
エントリーDOI | 10.2210/pdb1obq/pdb |
関連するPDBエントリー | 1GKA 1H91 1I4U 1OBU |
分子名称 | CRUSTACYANIN C1 SUBUNIT (2 entities in total) |
機能のキーワード | transport protein, lipocalin, antiparallel beta-strands, pigment |
由来する生物種 | HOMARUS GAMMARUS (EUROPEAN LOBSTER) |
細胞内の位置 | Secreted, extracellular space: P80029 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 41376.12 |
構造登録者 | Habash, J.,Boggon, T.J.,Raftery, J.,Chayen, N.E.,Zagalsky, P.F.,Helliwell, J.R. (登録日: 2003-01-31, 公開日: 2003-07-03, 最終更新日: 2011-07-13) |
主引用文献 | 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 Cited by 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: 12832753DOI: 10.1107/S0907444903007959 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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