1lyd: Difference between revisions

Revision as of 14:49, 21 February 2008

CRYSTAL STRUCTURE OF T4-LYSOZYME GENERATED FROM SYNTHETIC CODING DNA EXPRESSED IN ESCHERICHIA COLI

OverviewOverview

The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.

About this StructureAbout this Structure

1LYD is a Single protein structure of sequence from Bacteriophage t4. The following page contains interesting information on the relation of 1LYD with [Lysozyme]. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli., Rose DR, Phipps J, Michniewicz J, Birnbaum GI, Ahmed FR, Muir A, Anderson WF, Narang S, Protein Eng. 1988 Oct;2(4):277-82. PMID:3074306

Page seeded by OCA on Thu Feb 21 13:49:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==Overview==
-The polypeptide produced by expressing a chemically synthesized gene, coding for the amino-acid sequence of T4-lysozyme has been crystallized, and subjected to X-ray diffraction. The crystal structure has been refined, to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The, refined model is essentially the same as the well-known structure of, wild-type T4-lysozyme determined previously by Matthews et al. (1987)., Some small changes in the C-terminal region, which is important in, maintaining the folded structure, have been noted. In addition to, confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on, the folding and the catalytic activity of this molecule by the method of, gene synthesis.
+The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.
 ==About this Structure==
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 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Rose, D.R.]]
+[[Category: Rose, D R.]]
 [[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:21:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:33 2008''