1ja2

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(New page: 200px<br /><applet load="1ja2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ja2, resolution 2.87&Aring;" /> '''BINDING OF N-ACETYLG...)
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[[Image:1ja2.jpg|left|200px]]<br /><applet load="1ja2" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1ja2, resolution 2.87&Aring;" />
'''BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY'''<br />
'''BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY'''<br />
==Overview==
==Overview==
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The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C., 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at, room temperature. NAG was found to bind to lysozyme in a rapid, precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M, NaCl buffer pH 5.0. Binding was indicated by significant and readily, apparent changes in the diffraction pattern from that of the apo protein, precipitated from the same solvent. The location of NAG bound to lysozyme, was easily found from a difference Fourier map generated from structure, factors extracted during a preliminary combined Rietveld and, stereochemical restraint refinement. Full protein and protein-NAG, structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) =, 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG, which differed from that found in an earlier single-crystal study and, probably represents a precursor trapped by rapid precipitation.
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The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern from that of the apo protein precipitated from the same solvent. The location of NAG bound to lysozyme was easily found from a difference Fourier map generated from structure factors extracted during a preliminary combined Rietveld and stereochemical restraint refinement. Full protein and protein-NAG structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) = 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG which differed from that found in an earlier single-crystal study and probably represents a precursor trapped by rapid precipitation.
==About this Structure==
==About this Structure==
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1JA2 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=1JA2 OCA].
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1JA2 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=1JA2 OCA].
==Reference==
==Reference==
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dreele, R.B.Von.]]
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[[Category: Dreele, R B.Von.]]
[[Category: lysozyme]]
[[Category: lysozyme]]
[[Category: powder diffraction]]
[[Category: powder diffraction]]
[[Category: rietveld refinement]]
[[Category: rietveld refinement]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:02:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:23 2008''

Revision as of 11:20, 21 February 2008


1ja2, resolution 2.87Å

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BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY

Overview

The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern from that of the apo protein precipitated from the same solvent. The location of NAG bound to lysozyme was easily found from a difference Fourier map generated from structure factors extracted during a preliminary combined Rietveld and stereochemical restraint refinement. Full protein and protein-NAG structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) = 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG which differed from that found in an earlier single-crystal study and probably represents a precursor trapped by rapid precipitation.

About this Structure

1JA2 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.

Reference

Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study., Von Dreele RB, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1836-42. Epub 2001, Nov 21. PMID:11717496

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