Postdoctoral position - Sydney

[Joe Mack]

In article <1994Dec1.135622.1 at summer.chem.su.oz.au> guss_m at summer.chem.su.oz.au writes:
>Postdoctoral position in protein crystallography at Sydney

>e-mail: M.Guss at biochem.usyd.edu.au
>
>

Dear Mitch,

	I spoke to you by phone about 3 years ago when I was
trying by phone to track down and get the signature of Alex 
Wlodawer (who was visiting your lab) on a grant application form.
Through some mechanism, the details of which I've forgotten,
you solved my problem. Whether you remember this incident or not, 
I have no idea, but you helped me a lot, which I remember very well.

	I am a more senior person (47yrs old), and seeing the above posting,
I was wondering if there migh be any positions for a person like me. I 
have done a lot of protein work (kinetics, purification on 500mg scale, 
cloning, expression) as well as organic synthesis. 

	For the past few years I have been trying to parlay my 
experience in the protein area into learning crystallography. 	
My first structure is in progress - a homotetramer 4x55kd, P212121. 
I have a native data set to about 2.8A and am screening for metal 
derivatives (0/6 so far, all soaks are dead or native).

	I did my PhD with Michael Slaytor in Biochemistry at Sydney 
Uni after doing a BSc Hons in organic under Ern Ritchie. I have 
been in the US since. I was taught crystallography by Hans as
an undergrad. My most recent work has been with retroviral integrase
(==HIV), the enzyme which incorporates the pro-viral DNA into the 
host chromosome. After I'd cloned, expressed and purified large amounts of
the fully active integrase, I was hoping to try crystallising it, but 
that part of the project was given to someone else.

	I saw Hans when he was over here a few years ago and following
his talk on his Cu proteins, I made up a slide showing the sequence 
alignement with the height of each residue being the information 
content (p ln p) of that residue. The conserved residues are all 
full height and I drew a blue Cu atom in the middle of the alignment 
with bonds to the conserved residues. I don't know if you've seen 
the slide but Hans wrote back to me asking where I got all 
the sequences - I guess incase he'd missed any (which he hadn't).
I made this slide up as a more dramatic version of a slide which 
he used in his talk.

	If you would be interested, I could send you my CV and a more
formal letter of interest.

	Joe Mack
	(Nat Inst Health)
	mack at ncifcrf.gov