Sialic acids comprise a large family of nine-carbon amino sugars, all of which are derived from the parent compound N-acetyl neuraminic acid.  The enzyme N-acetyl neuraminate lyase (E.C. 4.1.3.3) is involved in the retro-aldol cleavage of N-acetyl neuraminic acid to form N-acetyl-D-mannosamine and pyruvate via a Schiff base intermediate. Recently, N-acetyl neuraminate lyase has received considerable attention from both mechanistic and structural viewpoints and has been recognised as a promising target for antibiotic development against pathogenic bacteria. The crystal structure of N-acetyl neuraminate lyase from methicillin-resistant Staphylococcus aureus has been solved to a resolution of 1.74 Å in the space group P21. When compared with small-angle X-ray scattering data, the crystal structure of N-acetyl neuraminate lyase depicts an accurate representation of the solution-based structure. Understanding the three-dimensional structure of N-acetyl neuraminate lyase in pathogenic bacteria, such as methicillin-resistant Staphylococcus aureus, will provide the preliminary information necessary for future antimicrobial development.