Protein Crystallization Hits

If I buy a reagent kit for my research, I need to know what's inside. Of course, how else can you carry out an experiment? I can not agree more with Anna Git's complaints in an Nature Comment that there is a lack of transparency imposed by some reagent manufacturers. (see Git, A. (2012). Research tools: A recipe for disaster Nature, 484 (7395), 439-440 DOI: 10.1038/484439a). Here are her grievances:

So here's our stance on this subject: Emerald Bio customers can get all recipe data that goes into any of our reagent kits. Most of this data is supplied in the various tech sheets. For instance, see here for a description of the 96 Wizard III/IV protein crystallization formulations. Should this information not be sufficient for you, call us toll free at 1-888-780-8588 and ask us what else you need. We're glad to share with you more detail on any of our protein crystallization formulations. For instance, recipes for formulations in any of our protein crystallization screens, down to the CAS number if you need, and even raw material supplier information. No need to whisper or sign any confidentiality agreements. 

Why are we doing this? Service to our customers who trust us as a no-formulation secrets manufacturer. And in the long run this openness is in our own interest: Your success in reproducible protein crystallization is our business. 

Thank you for your continued use of our products,

Peter

Protein researchers of the world: here's your chance to make a lasting impact with information, ideas and comments on the topic of future disruptive proteomics technologies. The NIH has an RFI (Request for Information, NOT-RM-12-015) out, asking you to provide input in to how to accelerate research in disruptive proteomics technologies.

There are simple online forms where you can provide your anonymous feedback on the following topics:

1. MS-based comprehensive protein identification and quantification. Realistic goals and associated challenges for orders-of-magnitude improvements in dynamic range, sensitivity, throughput or cost. Specific areas of instrumentation (e.g., source design/analyzer geometry, coupling with other instrumentation, etc.) more likely to yield disruptive improvements.
2. Non-MS-based comprehensive protein identification and quantification. Opportunities and challenges for other technologies that could in the near or far term approach/exceed MS-based methods with respect to: accuracy, dynamic range, throughput, and cost in analyzing proteomes.
3. Potential benefits and challenges in incorporation of informatics approaches and/or integration of large protein datasets into the development of the proteomic technologies.
4. Potential important impacts of proteomics technology breakthroughs in basic, discovery and translational biomedical research.

This unique opportunity is available until March 26.

          Quick! Disruptive proteomics technologies. The NIH wants to know what you're thinking.

What are you going to get out of this? No immediate grant awards. But your information may be included in planning  future grant funding opportunities that seek to fund disruptive technologies that have occurred in DNA sequencing technologies in the past few years.

And that impact may be larger than any of the papers you have ever published.

Exciting news that I need to share with you: the growing Emerald adopts a new name and leadership: 

We're Emerald Bio now:

The details of our transformation are given in this news release: Leading Proteomics Company Transitions to Emerald Bio, Chooses Key Leadership to Address Growing Market Opportunities

George Abe, new Chief Executive Officer and Peter Nollert, new Chief Technologist at Emerald Bio

We're looking forward to continuing to supply you with Emerald's protein crystallization screening kits, protein crystallization optimization reagents, stock solutions, protein crystallization plates and with sophisticated laboratory instrumentation such as the Opti Matrix Maker for the production of crystallization optimization matrices and the Protein Maker for parallel protien production. 

There's more to come.

Cheers,

Peter

This week I'll prepare my first Iodide soak ever. While we've determined many protein structures at Emerald BioStructures using anomalous data from iodide soaked crystals (see a previous blog post on this topic), I've never prepared iodide-soaked crystals myself. Being a novice I asked Tom Edwards who is an expert in this methodology. Turns out that he's preparing a webinar on this topic for next week: SAD phasing at rotating anode wavelengths using iodide ions. The goal of course is to obtain phases from anomalous X-ray diffraction data, the key to de-novo crystallographic structure determination. 

Tom Edwards on "SAD phasing at rotating anode wavelengths using iodide ions"

 I asked Tom for his 'standard iodide crystal soaking recipe'. Here is it:

1. prepare a 5 M Sodium Iodide stock and a formulation at 2 x of the crystallization cocktail.

2. Mix iodide to a final concentration of 1 M with the 2 x crystallization cocktail and include the cryo reagent.

3. Transfer a single crystal into 1 uL of 1 M soak and check for crystal damage. If there's no visible damage, test X-ray diffraction. Back down with the iodide concentration (0.75 M, 0.5 M etc.) if the quality of  X-ray diffraction  pattern suffers (mosaicity, resolution, split spots etc.).

4. Harvest, cool, mount, diffract, collect... 

The fun part - such as data treatment - will be covered in Tom's webinar

I'm off to the lab.

Peter

Congratulations to Robert G. Edwards to receiving the 2010 Nobel Prize for Physiology or Medicine. Robert is widely known for inventing and promoting the in vitro fertilization procedure. In a way he has 'fathered' 4 million people.

Not bad.

And here's a toast to Richard Heck, Ei-ichi Negishi and Akira Suzuki for receiving the 2010 Nobel Prize for Palladium-catalyzed couplings in organic synthesis.

I'll keep my fingers crossed for protein structural biology Nobels in 2011.

Cheers,

Peter