1obu
From Proteopedia
(New page: 200px<br /><applet load="1obu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obu, resolution 2.00Å" /> '''APOCRUSTACYANIN C1 C...) |
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| - | [[Image:1obu.gif|left|200px]]<br /><applet load="1obu" size=" | + | [[Image:1obu.gif|left|200px]]<br /><applet load="1obu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1obu, resolution 2.00Å" /> | caption="1obu, resolution 2.00Å" /> | ||
'''APOCRUSTACYANIN C1 CRYSTALS GROWN IN SPACE AND EARTH USING VAPOUR DIFFUSION GEOMETRY'''<br /> | '''APOCRUSTACYANIN C1 CRYSTALS GROWN IN SPACE AND EARTH USING VAPOUR DIFFUSION GEOMETRY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Models of apocrustacyanin C(1) were refined against X-ray data recorded on | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homarus_gammarus Homarus gammarus]. Full crystallographic information is available from [http:// | + | 1OBU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homarus_gammarus Homarus gammarus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homarus gammarus]] | [[Category: Homarus gammarus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boggon, T | + | [[Category: Boggon, T J.]] |
| - | [[Category: Chayen, N | + | [[Category: Chayen, N E.]] |
[[Category: Habash, J.]] | [[Category: Habash, J.]] | ||
| - | [[Category: Helliwell, J | + | [[Category: Helliwell, J R.]] |
[[Category: Raftery, J.]] | [[Category: Raftery, J.]] | ||
| - | [[Category: Zagalsky, P | + | [[Category: Zagalsky, P F.]] |
[[Category: antiparallel beta-strands]] | [[Category: antiparallel beta-strands]] | ||
[[Category: lipocalin]] | [[Category: lipocalin]] | ||
| Line 24: | Line 24: | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:50 2008'' |
Revision as of 12:15, 21 February 2008
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APOCRUSTACYANIN C1 CRYSTALS GROWN IN SPACE AND EARTH USING VAPOUR DIFFUSION GEOMETRY
Overview
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.
About this Structure
1OBU is a Single protein structure of sequence from Homarus gammarus. Full crystallographic information is available from OCA.
Reference
Apocrustacyanin C(1) crystals grown in space and on earth using vapour-diffusion geometry: protein structure refinements and electron-density map comparisons., Habash J, Boggon TJ, Raftery J, Chayen NE, Zagalsky PF, Helliwell JR, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1117-23. Epub 2003, Jun 27. PMID:12832753
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