1bwi: Difference between revisions

Revision as of 19:49, 30 June 2008

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File:1bwi.png

Template:STRUCTURE 1bwi

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

Template:ABSTRACT PUBMED 10089304

About this StructureAbout this Structure

1BWI is a Single protein structure of sequence from Gallus gallus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME'''
+===THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME===
-==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.
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+{{ABSTRACT_PUBMED_10089304}}
 ==About this Structure==
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 [[Category: 1,4-beta-n-acetylmuramidase c]]
 [[Category: Lysozyme]]
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