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Acta Crystallographica Section D: Biological Crystallography logoLink to Acta Crystallographica Section D: Biological Crystallography
. 2011 Nov 5;67(Pt 12):1076. doi: 10.1107/S0907444911045860

Crystallographic analysis of human hemoglobin elucidates the structural basis of the potent and dual antisickling activity of pyridyl derivatives of vanillin. Corrigendum

Osheiza Abdulmalik a, Mohini S Ghatge b, Faik N Musayev b, Apurvasena Parikh c, Qiukan Chen a, Jisheng Yang a, Ijeoma Nnamani d, Richmond Danso-Danquah b, Dorothy N Eseonu e, Toshio Asakura a, Donald J Abraham b, Jurgen Venitz c, Martin K Safo b,*
PMCID: PMC3337008

A correction to the paper by Abdulmalik et al. [(2011), Acta Cryst. D67, 920–928].

Keywords: hemoglobin, oxygen affinity, sickle-cell disease, polymerization, T state, R2 state, corrigendum

Abstract

The affiliation of one of the authors of Abdulmalik et al. (2011) [Acta Cryst. D67, 920–928] is corrected.


In the article by Abdulmalik et al. (2011) the affiliation of Toshio Asakura is incorrect. The correct affiliation is the Division of Hematology, The Children’s Hospital of Philadelphia, Philadelphia, USA, as given above.

References

  1. Abdulmalik, O., Ghatge, M. S., Musayev, F. N., Parikh, A., Chen, Q., Yang, J., Nnamani, I., Danso-Danquah, R., Eseonu, D. N., Asakura, T., Abraham, D. J., Venitz, J. & Safo, M. K. (2011). Acta Cryst. D67, 920–928. [DOI] [PMC free article] [PubMed] [Google Scholar]

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