Research Article

Crystallization and Structural Studies of Lysozyme from Hen Egg White, Using Vapour Diffusion Techniques

C.N. Fokunang, K.A. Watson, A. Purvis and E.A. Tembe-Fokunang

The aim of this study was to develop an in-house high throughput method of crystallization and structure determination of lysozyme enzyme as model in structure-based drug design studies. Lysozyme stock solution at 50 mg mL^-1 from hen egg white was crystallized using the vapour diffusion techniques in buffer A [0.1 M Na acetate/acetic acid pH 4.8, 0.2% Na azide (w/v), 1.1 M NaCl] and buffer B [0.1 M Na acetate/acetic acid pH 4.8, 0.02% Na azide (w/v), 25% ethylene glycol (w/v), 1.7 m M NaCl]. Two 24 well plates in duplicates were used for each buffer preparations and incubated at 4°C. High quality crystals between 0.2-0.5 mm sizes, were produced in buffer A plate well after days 2 of incubation and none in buffer B. The crystal data collection and refinement showed a high resolution of the outer shell of 2.28-1.92 Å, completeness of 98.7%, space group P4₃2₁2 and mosaicity of 0.415.

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C.N. Fokunang, K.A. Watson, A. Purvis and E.A. Tembe-Fokunang, 2005. Crystallization and Structural Studies of Lysozyme from Hen Egg White, Using Vapour Diffusion Techniques. Biotechnology, 4: 341-346.

DOI: 10.3923/biotech.2005.341.346

URL: https://scialert.net/abstract/?doi=biotech.2005.341.346

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Authors

C.N. Fokunang

K.A. Watson

A. Purvis

E.A. Tembe-Fokunang

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Research Article

Crystallization and Structural Studies of Lysozyme from Hen Egg White, Using Vapour Diffusion Techniques

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