Silpa's Projects

Summer Project 1999

I am currently a summer intern through a program sponsered by the DOE at the Stanford Linear Accelerator Center (SLAC).This is the homepage of the place where I work. The Stanford Synchrotron Radiation Laboratory (SSRL) is a part of SLAC and it is where I work. The picture of the lab can be seen below.

This lab consists of many different parts. The main part of the lab, SPEAR, can be seen above. It is a ring where all the electrons and positrons are stored. SPEAR stands for Stanford Positron Electron Accelerating Ring. The other ring is called the booster ring and it is where all the positrons and electrons are made. As these particles circle the ring, they produce synchrotron radiation beams (UV and x-ray photons). This is the world's most intense x-ray source!! (WOW). It enables the study of matter at the atomic or molecular scale of the surfaces of semiconductors or the structure of proteins. SPEAR actually provided enough information for Burton Richter to discover the fourth quark called the charm quark. This discovery led him to win the nobel. prize in physics in 1976. Pretty impressive don't you think?

Andrea and I are working on a protein crystallography project. She is also a fellow intern, chemistry major, and fan of Dawson's Creek. Check out her homepage for more about her life and our project. She does go to Harvard so her explanation might be better than mine.

We do our crystal work in a cold room at a temperature of 38 degrees Fahrenheit. We wear fleeces to keep us warm (see caption to the right). Who knew that sunny California could be so cold?

The crystallization of proteins first involves the use of a gel to grease the wells of the tray (see picture).

The crystals are grown from crygogenic or non-cryogenic solutions. The cryogenic or non-cryogenic solutions are put into the wells of the tray. A screen of cryo or non-cryo solutions is sometimes used to provide a varitey of conditions for the crystals to grow.

The wells are covered by glass coverslips with a drop of the protein and the well solution. Tweezers are used to transport the coverslips to ensure that it covers the well appropriately. The protein crystals should grow in the drops, if the conditions are ideal.

The picture to the right is of a finished well in the tray. It gives details about the well and the drop on the coverslip.

A cryo pin is used as a holder for the crystal. It has a small microscopic loop into which a 1/10 of a millimeter crystral should fit into. The pin is placed onto the goniometer head, and the beam then passes through the crystal.

The process of cooling crystals before they are analyzed in the beam is described in a powerpint presentation that was given to NASA. It can be seen at the following link... Powerpoint Presentation for NASA

X-rays that are provided by the Synchrotron Radiation are then used to probe the structure of the protein crystals. This information helps people to learn about the orientation of the electrons and other parts of the protein. The beamline, named 9-2, and the detector for the x-rays is shown here. From the data that the detector gives out, one can interpret the structure of the crystal.

The protein to be crystallized is horse skeletal myoglobin which can be seen to the right. We are also growing other types of protein crystals in case our myoglobin crystals do not turn out as well as expected. The other proteins are legmyglobin (found in plants) and arsenite oxidase (found in bacterium)

The Object of Our Research...

... is to find the optimum conditions to allow the protein crystals to grow. The different "cryo" conditions are prepared by varying the pH, temperature, ionic strength, and buffer of the well solutions.

As our final duty in the SISE program, we had to give a 20 minute presentation on our research this summer. This detailed deescription of protein crystallography can be seen at Final Powerpoint Presentation.

We do our crystal work in a cold room at a temperature of 38 degrees Fahrenheit. We wear fleeces to keep us warm (see caption to the right). Who knew that sunny California could be so cold?
The crystallization of proteins first involves the use of a gel to grease the wells of the tray (see picture).
The crystals are grown from crygogenic or non-cryogenic solutions. The cryogenic or non-cryogenic solutions are put into the wells of the tray. A screen of cryo or non-cryo solutions is sometimes used to provide a varitey of conditions for the crystals to grow.
The wells are covered by glass coverslips with a drop of the protein and the well solution. Tweezers are used to transport the coverslips to ensure that it covers the well appropriately. The protein crystals should grow in the drops, if the conditions are ideal.
The picture to the right is of a finished well in the tray. It gives details about the well and the drop on the coverslip.
A cryo pin is used as a holder for the crystal. It has a small microscopic loop into which a 1/10 of a millimeter crystral should fit into. The pin is placed onto the goniometer head, and the beam then passes through the crystal.
The process of cooling crystals before they are analyzed in the beam is described in a powerpint presentation that was given to NASA. It can be seen at the following link... Powerpoint Presentation for NASA
X-rays that are provided by the Synchrotron Radiation are then used to probe the structure of the protein crystals. This information helps people to learn about the orientation of the electrons and other parts of the protein. The beamline, named 9-2, and the detector for the x-rays is shown here. From the data that the detector gives out, one can interpret the structure of the crystal.
The protein to be crystallized is horse skeletal myoglobin which can be seen to the right. We are also growing other types of protein crystals in case our myoglobin crystals do not turn out as well as expected. The other proteins are legmyglobin (found in plants) and arsenite oxidase (found in bacterium)