I can only confirm what Alex said. And the structure was neither a globin or zyme or psin!

Victor


Quoting aaleshin <aales...@burnham.org>:

I and Victor Lamzin solved our first protein structure (3A resolution) in 80-s using pure MIR and a home made (Russian) diffractometer...

Alex

On Jun 6, 2012, at 1:42 PM, Boaz Shaanan wrote:

So if get the gist of the thread right, am I correct in assuming that the last protein structures to be solved strictly by MIR are haemoglobin/myoglobin, lysozyme and chymotrypsin and perhaps one or two more in the late sixties? In which case the answer to the original question about MIR being obsolete, is "yes it is since a long time"?

 Boaz


Boaz Shaanan, Ph.D.
Dept. of Life Sciences
Ben-Gurion University of the Negev
Beer-Sheva 84105
Israel

E-mail: bshaa...@bgu.ac.il
Phone: 972-8-647-2220  Skype: boaz.shaanan
Fax:   972-8-647-2992 or 972-8-646-1710





________________________________________
From: CCP4 bulletin board [CCP4BB@JISCMAIL.AC.UK] on behalf of Phil Evans [p...@mrc-lmb.cam.ac.uk]
Sent: Wednesday, June 06, 2012 6:04 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] Fun Question - Is multiple isomorphous replacement an obsolete technique?

No they were not useless! I used them

(probably better now with cryo data though)

Phil

On 6 Jun 2012, at 16:02, Dyda wrote:

I suspect that pure MIR (without anomalous) was always a fiction. I doubt that anyone has ever used it. Heavy atoms always give
an anomalous signal

Phil

I suspect that there was a time when the anomalous signal in data sets was fictional. Before the invent of flash freezing, systematic errors due to decay and the need of scaling together many derivative data sets collected on multiple crystals could render weak anomalous signal useless. Therefore MIR was needed. Also, current hardware/software
produces much better reduced data, so weak signals can become useful.

Fred

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