HIGH RESOLUTION STRUCTURE OF SPRUCE BUDWORM ANTIFREEZE PROTEIN

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The crystallization of spruce budworm antifreeze proteins have been crystallized with, unfortunately, many difficulties. Thin plate crystals can be obtained through repeated seedings (usually 3-6 times) and the reproducibility has been very low. Data collection using in-house x-ray facility has not been possible mainly due to the small size of the crystals. We were only able to collect data at CHESS. The crystal diffracted to maximum 2.2 A but the diffraction was highly anisotropic. In the "best" area, the diffraction is at 2.2 A but it goes down to 2.8 A in "worst" area. This is not too surprising because of the very thin edge of the plate crystals. At CHESS, we have collected a complete data set with reasonable qaulity to 2.6 A.