If i remember from last year i was in ireland cos it was quiet at home and every one was saying the same thing on this board how dead it was
in ireland at the moment its def quieter than usual but busier than what i would be at home though
you just have to put your head down and suck it and see literally
i never look at what i make each week /day rather at each month and it always works out to be the same roughly to a few hundred pounds either way
also save money for when its like this so that it not so much of panic stations when the money isnt coming in you still have some money stashed
the economic situation plus the fact that its xmas never help, i tend to find the week before xmas it picks up and then straight after as well it picks up as men are at home bored fuckless and have good excuse to get out of the house with no problems
keep your chin up it will all work out ok in the end