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Dear all, hopefully some of you may be able to make a few suggestions for a project I'm currently working on. It's a protein complex which crystallises to produce small crystals (max. dimension 0.1 mm, with rod morphology). It doesn't diffract in-house but does at synchrotron sources. The data is very anisotropic and a massive unit cell. I believe the indexing is P6 or P622 with cell dimensions 87.8, 87.8, 629.5. I've had a lot of problems scaling any data (I think, mainly due to overlaps or poor data and the anisotropy of diffraction). The crystals are frozen (but I do intend on trying some capillary mounted samples). Any suggestions regarding processing the data or optimising the data collection strategy would be wellcomed. If you would like to look at a typical frame collected at the ESRF on id23 at a distance of 445mm and a wavelength of 1.0 Ang. please feel free to download it from here: http://www.nottingham.ac.uk/~pazxtal Regards, Paul.. ################################## Dr Paul A. McEwan Post-Doctoral Research Fellow Protein Crystallography Group Centre for Biomolecular Science Clifton Boulevard University of Nottingham Nottingham NG7 2RD Tel: 0115 8468009 http://www.nottingham.ac.uk/~pazxtal ################################## This message has been checked for viruses but the contents of an attachment may still contain software viruses, which could damage your computer system: you are advised to perform your own checks. Email communications with the University of Nottingham may be monitored as permitted by UK legislation.
