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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001646-16
Application #
6281274
Study Section
Project Start
1998-09-15
Project End
1999-08-14
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
16
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Cornell University
Department
Type
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850
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