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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.

Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 A. The crystal contains three molecules in an asymmetric unit (VM = 2.11 A3 Da(-1)) and has a solvent content of 61.5%.[1]

References

  1. Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus. Nagata, K., Tsutsui, S., Lee, W.C., Ito, K., Kamo, M., Inoue, Y., Tanokura, M. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
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