3lz2

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{{STRUCTURE_3lz2| PDB=3lz2 | SCENE= }}
{{STRUCTURE_3lz2| PDB=3lz2 | SCENE= }}
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'''STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION'''
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===STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION===
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==Overview==
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The three-dimensional structure of turkey egg-white lysozyme (TEWL) has been solved and refined at 2.5 A resolution using X-ray data collected by the Laue method. This is the first protein structure determination undertaken using Laue diffraction data. A re-examination of the existing structure of TEWL was necessary when attempts to refine an atomic model based on the C alpha positions in the Protein Data Bank (entry 1LZ2) failed. The correct orientation and position of the turkey lysozyme molecules within the crystallographic unit cell were determined by molecular replacement using a refined model of the homologous hen egg-white lysozyme crystal structure. After modification of the model to reflect the differences in amino-acid sequence between the chicken and turkey enzymes, the structure was subjected to crystallographic refinement using the simulated-annealing refinement technique and conventional least-squares refinement. This yielded a final residual of R = 20.7%. This crystal form is of potential interest for time-resolved crystallographic studies since the amino-acid residues involved in catalysis (Asp52 and Glu35) are accessible to solvent and not blocked by crystal contacts.
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{{ABSTRACT_PUBMED_1515108}}
==About this Structure==
==About this Structure==
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[[Category: Parsons, M R.]]
[[Category: Parsons, M R.]]
[[Category: Petsko, G A.]]
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Revision as of 09:54, 3 July 2008

Image:3lz2.png

Template:STRUCTURE 3lz2

STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION

Template:ABSTRACT PUBMED 1515108

About this Structure

3LZ2 is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.

Reference

Structure determination of turkey egg-white lysozyme using Laue diffraction data., Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA, Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):200-7. PMID:1515108

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