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Cook, W.J. et al.

Crystallization and preliminary X-ray investigation of a ubiquitin carrier protein (E2) from Arabidopsis thaliana.

Crystals of a recombinant ubiquitin carrier protein from Arabidopsis thaliana have been grown from solutions of ammonium sulfate. The crystals are orthorhombic, space group P2(1)2(1)2(1); the axes are a = 41.8(1) A, b = 44.9(1) A and c = 83.2(1) A. The crystals are quite stable to X-rays and diffract beyond 2.1 A resolution. There is one molecule in the asymmetric unit.[1]

References

Crystallization and preliminary X-ray investigation of a ubiquitin carrier protein (E2) from Arabidopsis thaliana. Cook, W.J., Jeffrey, L.C., Sullivan, M.L., Vierstra, R.D. J. Mol. Biol. (1992) [Pubmed]

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