HIGH RESOLUTION STRUCTURE OF SPRUCE BUDWORM ANTIFREEZE PROTEIN

云杉夜蛾抗冻蛋白的结晶 不幸的是，它的结晶遇到了很多困难。 薄板 通过反复沉淀（通常3-6次）可获得晶体。 并且可重复性非常低。 数据收集使用 无法建立内部X光设施，主要原因是 晶体的大小。 我们只能在国际象棋中收集数据。 该晶体衍射至最大2.2 A，但衍射强度很高。 各向异性 在“最佳”区域中，衍射在2.2 A处，但它 在“最差”区域下降到2.8 A。 这并不太令人惊讶 因为片状晶体的边缘非常薄。 在国际象棋，我们 已收集到一套完整的数据集，质量合理，达到2.6A。

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.