3lz2
From Proteopedia
|
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. Active as Lysozyme, with EC number 3.2.1.17 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 Tue Nov 20 19:50:26 2007
