Spectrum mill proteomics software

Structural protein analysis was performed as described previously4 (link). Briefly, the purified phage particles were heat-denaturized and loaded onto a 15% (w/v) polyacrylamide gel to visualize PaoP5 structural proteins. SDS–PAGE (12% [w/v] and 10% [w/v]) was also performed to better separate proteins with different molecular weights. Proteins were stained with Coomassie Brilliant Blue R250 dye and washed with methanol–acetic acid–H₂O. Then, protein bands were excised from the gel for HPLC–MS analysis. The data from HPLC–MS analysis were processed by Agilent Spectrum Mill proteomics software to allocate each band to the corresponding gene.

Proteomic analysis was performed as previously described23 (link). Briefly, purified particles were denatured with heat and loaded onto a 15% (w/v) polyacrylamide gel. Proteins were stained with Coomassie Brilliant Blue R250 dye and washed with methanol–acetic acid–H2O.
To identify phage structural proteins, we performed the above mentioned experiment for 30 min. The protein band that included all the structural proteins was excised from the gel for HPLC-MS analysis. HPLC-MS data were processed by the Agilent Spectrum Mill proteomics software to allocate each protein to the corresponding gene.