1lzt

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(New page: 200px<br /><applet load="1lzt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lzt, resolution 1.97&Aring;" /> '''REFINEMENT OF TRICLI...)
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[[Image:1lzt.gif|left|200px]]<br /><applet load="1lzt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lzt, resolution 1.97&Aring;" />
caption="1lzt, resolution 1.97&Aring;" />
'''REFINEMENT OF TRICLINIC LYSOZYME'''<br />
'''REFINEMENT OF TRICLINIC LYSOZYME'''<br />
==Overview==
==Overview==
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X-ray diffraction data to 1.5 A resolution have been collected for, triclinic crystals of hen egg white lysozyme. The triclinic model was, derived from the tetragonal one by the rotation function and refined, initially by Fo-Fc and differential difference syntheses against 2 A, resolution data. Refinement was continued by differential difference, cycles against the 1.5 A data until R was reduced to 0.220. Although the, initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic, error which affected primarily the high-resolution data. Refinement was, continued against the corrected 2 A data by block-diagonal least squares., After five cycles the refinement was terminated at R = 0.254 because of, the imminent availability of a preferred refinement program. Problems with, the protein model, the solvent, and the interaction of the scale and, thermal parameters are discussed. The experiences gained in this study are, summarized.
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X-ray diffraction data to 1.5 A resolution have been collected for triclinic crystals of hen egg white lysozyme. The triclinic model was derived from the tetragonal one by the rotation function and refined initially by Fo-Fc and differential difference syntheses against 2 A resolution data. Refinement was continued by differential difference cycles against the 1.5 A data until R was reduced to 0.220. Although the initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic error which affected primarily the high-resolution data. Refinement was continued against the corrected 2 A data by block-diagonal least squares. After five cycles the refinement was terminated at R = 0.254 because of the imminent availability of a preferred refinement program. Problems with the protein model, the solvent, and the interaction of the scale and thermal parameters are discussed. The experiences gained in this study are summarized.
==About this Structure==
==About this Structure==
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1LZT 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=1LZT OCA].
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1LZT 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=1LZT OCA].
==Reference==
==Reference==
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Brown, G.M.]]
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[[Category: Brown, G M.]]
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[[Category: Hodsdon, J.M.]]
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[[Category: Hodsdon, J M.]]
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[[Category: Jensen, L.H.]]
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[[Category: Jensen, L H.]]
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[[Category: Sieker, L.C.]]
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[[Category: Sieker, L C.]]
[[Category: hydrolase(o-glycosyl)]]
[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:01:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:59 2008''

Revision as of 11:50, 21 February 2008


1lzt, resolution 1.97Å

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REFINEMENT OF TRICLINIC LYSOZYME

Overview

X-ray diffraction data to 1.5 A resolution have been collected for triclinic crystals of hen egg white lysozyme. The triclinic model was derived from the tetragonal one by the rotation function and refined initially by Fo-Fc and differential difference syntheses against 2 A resolution data. Refinement was continued by differential difference cycles against the 1.5 A data until R was reduced to 0.220. Although the initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic error which affected primarily the high-resolution data. Refinement was continued against the corrected 2 A data by block-diagonal least squares. After five cycles the refinement was terminated at R = 0.254 because of the imminent availability of a preferred refinement program. Problems with the protein model, the solvent, and the interaction of the scale and thermal parameters are discussed. The experiences gained in this study are summarized.

About this Structure

1LZT 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

Refinement of triclinic lysozyme: I. Fourier and least-squares methods., Hodsdon JM, Brown GM, Sieker LC, Jensen LH, Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):54-62. PMID:2302326

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