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1 with unit cell parameters a = 66.2 Å, b = 77.6 Å, c = 86.6 Å. For data collection, crystals were soaked for ∼5 minutes in 20 percent glycerol, 80 percent mother liquor, and then frozen by plunging into liquid nitrogen. Data were collected at the Stanford Synchrotron Radiation Laboratory (SSRL) to a maximum resolution of 2.1 Å. The data were integrated and merged with the DENZO/SCALE-PACK package (32). The structure was determined by molecular replacement using a modified mature 48G7 with hapten structure (10). The nine somatic point mutations were replaced as alanines and used as a search model. The rotation and translation search was performed with AMORE (33). Both germline data sets provided a strong peak solution and the best solution was placed into the program X-PLOR (34) for rigid-body minimization. The model was completed with several cycles of molecular dynamics by X-PLOR and subsequent model building with program O (35). Free R values were monitored throughout the model-building. A bulk solvent correction was applied with the X-PLOR. All CDR loops were omitted and rebuilt into density, and the hapten was fitted into the germline with the hapten data set (Table 1). Model quality was checked using the program PROCHECK (36).
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24
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1842359733
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note
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κ constant regions, respectively (37).
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H rotation angle was calculated [R. L. Stanfield, M. Kamimura, J. M. Rini, A. T. Profy, I. A. Wilson Structure 1, 83 (1993)]. The heavy chains of two Fab variable domains were superimposed by the program XPLOR (34). The rotation angle was defined as the rotation angle required to bring the light chains into coincidence.
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We thank I. Wilson, B. Spiller, and B. Santarsiero for helpful comments on the manuscript. Supported by DOE contract DEACO3765F00098 (P.G.S.), NIH grant R01 AI39089 (R.C.S.), and the Howard Hughes Medical Institute (P.G.S.). We thank the Stanford Synchrotron Radiation Laboratory for Synchrotran beamtime. The coordinates have been deposited in the protein data bank with accession numbers 1AJ7and2RCS.
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