TY - JOUR
T1 - Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 Å resolution
T2 - Comparison with results from isothermal titration calorimetry
AU - Cohen, Gerson H.
AU - Silverton, Enid W.
AU - Padlan, Eduardo A.
AU - Dyda, Fred
AU - Wibbenmeyer, Jamie A.
AU - Willson, Richard C.
AU - Davies, David R.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/5
Y1 - 2005/5
N2 - The structure of the complex between hen egg-white lysozyme and the Fab HyHEL-5 at 2.7 Å resolution has previously been reported [Cohen et al. (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant Fab, the X-ray structure of the complex has been re-evaluated at 1.7 Å resolution. The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. The model of the full complex has improved significantly, yielding an R work of 19.5%. With this model, the structural results can be compared with the results of isothermal titration calorimetry. An attempt has been made to estimate the changes in bound waters that accompany complex formation and the difficulties inherent in using the crystal structures to provide the information necessary to make this calculation are discussed.
AB - The structure of the complex between hen egg-white lysozyme and the Fab HyHEL-5 at 2.7 Å resolution has previously been reported [Cohen et al. (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant Fab, the X-ray structure of the complex has been re-evaluated at 1.7 Å resolution. The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. The model of the full complex has improved significantly, yielding an R work of 19.5%. With this model, the structural results can be compared with the results of isothermal titration calorimetry. An attempt has been made to estimate the changes in bound waters that accompany complex formation and the difficulties inherent in using the crystal structures to provide the information necessary to make this calculation are discussed.
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U2 - 10.1107/S0907444905007870
DO - 10.1107/S0907444905007870
M3 - Article
C2 - 15858274
AN - SCOPUS:22844444097
SN - 0907-4449
VL - 61
SP - 628
EP - 633
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 5
ER -