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Lateral mapping of the X-ray absorption structure of a metalloprotein in a liquid cell by transmission electron microscopy technology (CAT#: STEM-MIT-0019-LJX)

Introduction

Metalloproteins are formed by the combination of proteins and metal ions. Most of the metal ions are only bound to proteins; A few are bound to a smaller molecule in addition to a protein, for example, iron (Ⅱ) in hemoglobin is bound to porphyrins in addition to proteins. Metallic proteins have important physiological functions. Hemoglobin, for example, is necessary to carry oxygen. Ceruloplasmin can catalyze the oxidation of iron (Ⅱ) to facilitate the combination of iron (Ⅲ) and protein to form ferritin. Ferritin is used to transport iron. Ferritin is used to store iron and so on.




Principle

Transmission electron microscopy (TEM) is to project the accelerated and concentrated electron beam onto a very thin sample, and the electron collides with the atoms in the sample and changes the direction, thus generating the stereo scattering Angle. The size of the scattering Angle is related to the density and thickness of the sample, so the image can be formed with different shades. The image can be enlarged, focused and displayed on imaging devices such as fluorescent screens, film and photosensitive coupling components. The resolution of transmission electron microscope is much higher than that of optical microscope, can reach 0.1~0.3nm, magnification of tens of thousands to millions of times. Therefore, transmission electron microscopy can be used to observe the fine structure of the sample.

Applications

Microscopic imaging in materials science or biology.

Procedure

1. Sampling
2. Preparation of slices
3. Staining (Select according to the specific experimental situation)
4. Observation

Materials

• Sample Type:
Liquid cell

Notes

Pay attention to air humidity
Voltage needs to be stabilized