1bwi
THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
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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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