Michael (and some others)

You haven't mentioned - and I guess don't use regularly - the "random" MMS
approach, where crushed seed-crystals are added to random screens.  This
really is a terrific method, and it will on average roughly double
productivity.  It's the first thing I would think of in a case like
Vijaykumar's (as I told him this morning!).

Galina Obmolova and her colleagues published a great paper earlier this
year about MMS.  They were working with a set of 16 Fab fragments that
comprised all combinations of 4 different heavy chains and 4 different
light chains.  Three structures were generated without MMS, but by various
very creative uses of microseeding they were able to get all 16/16
structures.  Ref below.

Best wishes,

Patrick

__________________________


Obmolova, G., Malia, T. J., Teplyakov, A., Sweet, R. W., & Gilliland, G. L.
(2014). Protein crystallization with microseed matrix screening:
application to human germline antibody Fabs. *Structural Biology and
Crystallization Communications*, *70*(8).




On 31 October 2014 16:07, R. M. Garavito <[email protected]> wrote:

> Although three months is a long time, it is no completely unheard of, and
> does not require the invocation of proteolysis.  The longest time I have
> heard of is ~1 yr, so count yourself lucky.  However to get good advice, as
> well as to use it, you need to ask yourself several questions:
>
> 1.  What kind of crystals are they?  Protein, salt, etc? If they are salt,
> don't pursue this condition.
>
> 2.  How many crystals did you get?  One or 2 in a drop or a microcrystal
> shower. And of what kind?  Single, well shaped, rosettes, needle clusters,
> or something that looks crystalline.  Screen more broadly around your
> initial hit.
>
> 3.  How many times have your tried to repeat this?  Once, twice, or more?
> Did you try setups in duplicate?  If so, did you get reproducible results?
> Have you actually screened around these conditions, varying each component
> systematically (PEG, salt, pH, buffer, etc.)?
>
> 4.  What method did you use? And in what kind of container?  For one
> thing, we don't completely trust the integrity of our setups for longer
> than 2 months.  All containers leak water slowly, so when crystals take
> longer than 2 months to grow (a) the real conditions are at much higher
> values than you naively think (i.e., the drop has dried out more than you
> expected) or (b) other components are crystallizing, for example a zinc
> salt.  It depends what else is in your protein buffer, as well.
>
> To quicken protein crystallization (which is not always a good thing),
> increase your protein concentration (by 1.5-2x) and/or PEG concentration
> (such as screening up to 40% PEGmme 550).  Sadly, crystallization is a
> combination of thermodynamic and kinetic factors:  you can get crystals
> (sometimes a single crystal only) when just outside the truly optimal
> conditions, but this may be only a sporadic event. You got to keep
> screening.
>
> Good luck,
>
> Michael
>
>
> ******************************************************************
> *R. Michael Garavito, Ph.D.*
> *Professor of Biochemistry & Molecular Biology*
> *603 Wilson Rd., Rm. 513*
> *Michigan State University      *
> *East Lansing, MI 48824-1319*
> *Office:*  *(517) 355-9724     Lab:  (517) 353-9125*
> *FAX:  (517) 353-9334        Email:  [email protected]
> <[email protected]>*
> ******************************************************************
>
>
>
>
> On Oct 31, 2014, at 6:05 AM, Vijaykumar Pillalamarri <
> [email protected]> wrote:
>
> Dear all,
>
> I am trying to crystallize a 30 kD protein. Protein crystals are formed
> after 3 months. The crystals are formed in the following condition:
> 0.01M Zinc sulphate
> 0.1M MES monohydrate pH 6.5
> 25% v/v PEG monomethyl ether 550
>
> Please suggest me how to grow these crystals faster.
>
> Thanking you
>
> --
> Vijaykumar Pillalamarri,
> UGC-JRF,
> C/O: Dr. Anthony Addlagatta,
> Senior Scientist,
> CSIR-IICT, Tarnaka,
> Hyderabad, India-500007
> Mobile: +918886922975
>
>
>


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