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Apocrustacyanin A1 from the lobster carotenoprotein α-crustacyanin: crystallization and initial X-ray analysis involving softer X-rays
Chayen, N.E.; Cianci, M.; Olczak, A.; Raftery, J.; Rizkallah, P.J.; Zagalsky, P.F.; Helliwell, J.R. (2000). Apocrustacyanin A1 from the lobster carotenoprotein α-crustacyanin: crystallization and initial X-ray analysis involving softer X-rays. Acta Crystallogr. Sect. D 56(8): 1064-1066. https://dx.doi.org/10.1107/s0907444900008556
In: Acta Crystallographica Section D-Structural Biology. International Union of Crystallography: Oxford. ISSN 2059-7983, meer
Peer reviewed article  
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  • Chayen, N.E.
  • Cianci, M.
  • Olczak, A.
  • Raftery, J.
  • Rizkallah, P.J.
  • Zagalsky, P.F.
  • Helliwell, J.R.
Abstract
    The A1 subunit of the carotenoprotein α‐crustacyanin, isolated from lobster carapace, has been crystallized using the vapour‐diffusion method. The crystals, grown in solutions of ammonium sulfate containing methylpentanediol (MPD), diffracted to 2.0 Å. The crystals are stable to radiation. The space group of the crystals is P212121. The unit‐cell parameters are a = 41.9, b = 80.7, c = 110.8 Å. `Standard structure determination' has been unsuccessful within this crustacyanin family. Instead, an approach based on the S atoms is being undertaken involving softer X‐rays at the SRS, Daresbury.
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