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 | STRUCTURAL BIOLOGY |
Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid. Erratum
aAvidis S.A., Biopôle Clermont-Limagne, 63360 Saint-Beauzire, France, bIBCP–Laboratoire de Bio-Cristallographie, 7 Passage du Vercors, 69367 Lyon CEDEX 07, France, cEuropean Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble CEDEX, France, and dInstitut de Biologie Structurale Jean-Pierre Ebel, CEA/CNRS/UJF, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX 1, France
*Correspondence e-mail: jouve@ibs.fr
In the paper by Andreoletti et al. [(2003), Acta Cryst. D59, 2163–2168] an incorrect version of Figure 2 was published. The correct version is given below![[link]](../../../../../../logos/arrows/d_arr.gif)
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![[Figure 2]](hv9001fig1thm.gif) | Figure 2 Close-up view of the active-site region of the native, compound I and formic acid complex structures of PMC. These three structures are coloured light grey, grey and black, respectively, and are drawn in stereo. Haem Fe atoms are represented as large balls. Water molecules and the O atom of the compound I oxoferryl group are displayed as small balls. The formic acid molecule is represented as black sticks. |
Keywords: P. mirabilis catalase; formic acid; compound I.
References
Andreoletti, P., Pernoud, A., Sainz, G., Gouet, P., Jouve, H. M. (2003). Acta Cryst. D59, 2163–2168. Web of Science CrossRef CAS IUCr Journals Google Scholar
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