1obu: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1obu.gif|left|200px]]<br /><applet load="1obu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1obu, resolution 2.00&Aring;" />
caption="1obu, resolution 2.00&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBU OCA].  
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==
Line 13: Line 13:
[[Category: Homarus gammarus]]
[[Category: Homarus gammarus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Boggon, T.J.]]
[[Category: Boggon, T J.]]
[[Category: Chayen, N.E.]]
[[Category: Chayen, N E.]]
[[Category: Habash, J.]]
[[Category: Habash, J.]]
[[Category: Helliwell, J.R.]]
[[Category: Helliwell, J R.]]
[[Category: Raftery, J.]]
[[Category: Raftery, J.]]
[[Category: Zagalsky, P.F.]]
[[Category: Zagalsky, P F.]]
[[Category: antiparallel beta-strands]]
[[Category: antiparallel beta-strands]]
[[Category: lipocalin]]
[[Category: lipocalin]]
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[[Category: transport protein]]
[[Category: transport protein]]


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