3lz2

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[[Image:3lz2.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_3lz2", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lz2 OCA], [http://www.ebi.ac.uk/pdbsum/3lz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3lz2 RCSB]</span>
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'''STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION'''
'''STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION'''
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[[Category: Parsons, M R.]]
[[Category: Parsons, M R.]]
[[Category: Petsko, G A.]]
[[Category: Petsko, G A.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:06:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:34:35 2008''
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Revision as of 19:06, 4 May 2008

Image:3lz2.jpg

Template:STRUCTURE 3lz2

STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION


Overview

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.

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 Page seeded by OCA on Sun May 4 22:06:30 2008

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