3ngg

Publication Abstract from PubMed

The 50-residue snake venom protein L-omwaprin and its enantiomer D-omwaprin were prepared by total chemical synthesis. Radial diffusion assays were performed against Bacillus megaterium and Bacillus anthracis; both L-omwaprin and D-omwaprin showed anti-bacterial activity against B. megaterium. The native protein enantiomer, made of L- amino acids, failed to crystallize readily. However, when a racemic mixture containing equal amounts of L-omwaprin and D-omwaprin was used, diffraction quality crystals were obtained. The racemic protein sample crystallized in the centrosymmetric space group P2(1)/c and its structure was determined at atomic resolution (1.33 A) by a combination of Patterson and direct methods based on the strong scattering from the sulfur atoms in the eight cysteine residues per protein. Racemic crystallography once again proved to be a valuable method for obtaining crystals of recalcitrant proteins, and for determining high resolution X-ray structures by direct methods.

Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography.,Banigan JR, Mandal K, Sawaya MR, Thammavongsa V, Hendrickx AP, Schneewind O, Yeates TO, H Kent SB Protein Sci. 2010 Jul 28. PMID:20669184^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.