3LZ2

STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION

Summary for 3LZ2

• Entry DOI: 10.2210/pdb3lz2/pdb
• Descriptor: TURKEY EGG WHITE LYSOZYME (1 entity in total)
• Functional Keywords: hydrolase(o-glycosyl)
• Biological source: Meleagris gallopavo (turkey)
• Total number of polymer chains: 1
• Total formula weight: 14228.10

Authors

Howell, P.L.,Almo, S.C.,Parsons, M.R.,Hajdu, J.,Petsko, G.A. (deposition date: 1991-09-13, release date: 1993-10-31, Last modification date: 2024-10-09)

Primary citation

Howell, P.L.,Almo, S.C.,Parsons, M.R.,Hajdu, J.,Petsko, G.A.
Structure determination of turkey egg-white lysozyme using Laue diffraction data.
Acta Crystallogr.,Sect.B, 48:200-207, 1992

PubMed Abstract: 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.

PubMed: 1515108
DOI: 10.1107/S0108768191012466

Experimental method

X-RAY DIFFRACTION (2.5 Å)