Axs platinum 135 ccd detector

X-ray data sets were collected in house using a Bruker AXS Platinum 135 CCD detector controlled with the Proteum software suite (Bruker AXS Inc.) The X-ray source was Cu Kα radiation from a Rigaku RU200 X-ray generator equipped with Montel optics and operated at 50 kV and 90 mA. The X-ray data sets were processed with SAINT and scaled with SADABS (Bruker AXS Inc.). Relevant X-ray data collection statistics are listed in Table 1.
The structure of KdnA was determined via molecular replacement using the software package PHASER,^{11 (link)} with the coordinates of QdtB serving as the search model.^{12 (link)} 4-fold averaging and solvent flattening yielded an electron density map that allowed for essentially a complete tracing of the KdnA polypeptide chain. The model was subjected to alternate cycles of refinement with REFMAC^{13 (link)} and manual model building with COOT.^{14 (link),15 (link)} KdnB was also solved using PHASER with the search model being that of PDB entry 3RF7. The KdnB model was refined in a similar manner as that for KdnA. Model refinement statistics are listed in Table 2.

All of the X-ray data sets were collected in house with a Bruker AXS Platinum-135 CCD detector controlled with the PROTEUM software suite (Bruker AXS Inc.) The X-ray source was Cu Kα radiation from a Rigaku RU200 X-ray generator equipped with Montel optics and operated at 50 kV and 90 mA. The X-ray data sets were processed with SAINT and scaled with SADABS (Bruker AXS Inc.). Relevant X-ray data collection statistics are listed in Table 1.
All structures of the E395A mutant variants were solved via molecular replacement with the software package PHASER using as a search probe the FdtF coordinates determined at 3.0 Å resolution. Iterative cycles of model-building with COOT (Emsley and Cowtan, 2004 (link); Emsley et al., 2010 (link)) and refinement with REFMAC (Murshudov et al., 1997 (link)) were employed to produce the final X-ray coordinate files. Model refinement statistics are provided in Table 2.