1bwi: Difference between revisions

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New page: left|200px<br /><applet load="1bwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwi, resolution 1.80Å" /> '''THE 1.8 A STRUCTURE ...
 
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[[Image:1bwi.gif|left|200px]]<br /><applet load="1bwi" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bwi, resolution 1.80&Aring;" />
caption="1bwi, resolution 1.80&Aring;" />
'''THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME'''<br />
'''THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME'''<br />


==Overview==
==Overview==
A number of methods can be used to improve the stability of the protein, crystal-growth environment, including growth in microgravity without an, air-liquid phase boundary, growth in gels and growth under oil, ('microbatch'). In this study, X-ray data has been collected from and, structures refined for crystals of hen egg-white lysozyme (HEWL) grown, using four different methods, liquid-liquid dialysis on Earth and in, microgravity using the European Space Agency's (ESA) Advanced Protein, Crystallization Facility (APCF) on board the NASA Space Shuttle Life and, Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose, gel using a tube liquid-gel diffusion method and crystallization in, microbatch under oil. A comparison of the overall quality of the X-ray, data, the protein structures and especially the bound-water structures has, been carried out at 1.8 A. The lysozyme protein structures corresponding, to these four different crystallization methods remain similar. A small, improvement in the bound-solvent structure is seen in lysozyme crystals, grown in microgravity by liquid-liquid dialysis, which has a more stable, fluid physics state in microgravity, and is consistent with a better, formed protein crystal in microgravity.
A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.


==About this Structure==
==About this Structure==
1BWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWI OCA].  
1BWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWI OCA].  


==Reference==
==Reference==
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bi, R.C.]]
[[Category: Bi, R C.]]
[[Category: Boggon, T.J.]]
[[Category: Boggon, T J.]]
[[Category: Chayen, N.E.]]
[[Category: Chayen, N E.]]
[[Category: Dong, J.]]
[[Category: Dong, J.]]
[[Category: Raftery, J.]]
[[Category: Raftery, J.]]
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[[Category: lysozyme]]
[[Category: lysozyme]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:58:29 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:48 2008''

Revision as of 12:59, 21 February 2008

File:1bwi.gif


1bwi, resolution 1.80Å

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THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME

OverviewOverview

A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.

About this StructureAbout this Structure

1BWI is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution., Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:10089304

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