Diff for "MichaelBell"

Differences between revisions 26 and 27

Michael Bell, Ludtke Lab (2014 - 2019)

All are welcome to use the materials provided here. Credit is appreciated but not required.

Thesis

Note: All protein illustrations in are licensed under a Creative Commons Attribution 4.0 International license by David S. Goodsell and the RCSB PDB.

Thesis Defense Presentation

defense_slides.key

Posters

cryoet_poster.pdf, cryoet_poster.pptx

scbmb_retreat_2016.pdf

biochem_retreat_2016.pdf

biophysical_society_2017.pdf

keck_arc_2017.pdf

sealy_2018.pdf

Note, these posters are have been uploaded without modification. There may be typos.

Talks

mapchallenge_wrapup_2017.key

microscopy_microanalysis_2018.ppt

Select Thesis Figures

Structural biology overview

Transmission electron microscopes (TEM)

TEM grids

Movie-mode imaging

Basic image processing

Fourier transforms

Single particle analysis

Contrast transfer function (CTF)

Resolution measurement via Fourier Shell Correlation (FSC)

Electron cryo-tomography (cryoET)

Subtomogram Averaging / Single particle tomography (SPT)

-  ⇤ ← Revision 26 as of 2019-04-04 15:45:19 → 
  Size: 3313
  Editor: MichaelBell
  Comment:
+   ← Revision 27 as of 2019-04-04 15:47:26 → ⇥
  Size: 1925
  Editor: MichaelBell
  Comment:
-Deletions are marked like this.
+Additions are marked like this.
 Line 39:
+Structural biology overview
-Line 41:
+Line 42:
-A. Example proteins. 1. Ribosomes such as this use the information encoded in ribonucleic acid (RNA) to assemble amino acids into chains, forming other protein structures. 2. Membrane transporters such as the TolC-AcrAB complex shown here move molecules across cellular membranes, helping maintain homeostatic conditions. 3. Enzymes. Shown here are a set of glycolytic enzymes that break down sugars to produce energy for cellular functions in the form of adenosine triphosphate (ATP) molecules. B. Length scales. Structural biology studies topics spanning a wide range of length scales from cells, which span multiple microns to atoms and small molecules, spanning only a few angstroms. While objects larger than ~200 nm can be examined using a light microscope, higher-resolution techniques such as X-ray crystallography (XRC), nuclear magnetic resonance (NMR), and electron microscopy are required to visualize features ranging from protein complexes to individual atoms. C. Taxonomy of protein structure elements superimposed on a structure of hemoglobin (PDB 2HHB). Protein structures are taxonomized according to their primary, secondary, tertiary, and quaternary structure elements. A protein’s primary structure corresponds to its sequence of amino acids. Secondary structure assigns spatial relationships between sequence elements, forming motifs such as the alpha-helix shown in this example. Tertiary structure describes how secondary structure elements conform within a single chain, and quaternary structure describes how multiple amino acid chains combine to form a complex.

Protein illustrations in A and B are licensed under a Creative Commons Attribution 4.0 International license by David S. Goodsell and the RCSB PDB.
+Transmission electron microscopes (TEM)
-Line 47:
+Line 45:
+TEM grids
-Line 49:
+Line 48:
+Movie-mode imaging
 Line 51:
+Basic image processing
-Line 53:
+Line 54:
+Fourier transforms
-Line 55:
+Line 57:
+Single particle analysis
-Line 57:
+Line 60:
+Contrast transfer function (CTF)
-Line 59:
+Line 63:
+Resolution measurement via Fourier Shell Correlation (FSC)
-Line 61:
+Line 66:
+Electron cryo-tomography (cryoET)
-Line 63:
+Line 69:
+Subtomogram Averaging / Single particle tomography (SPT)