Difference: CemProtocEC (1 vs. 14)

Revision 1426 Oct 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"
Return to Cryo EM web page at http://www.nysbc.org/facilities/CEM

Principles & Protocols

Principles - Electron crystallography

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Jump to Protocol

 

In order to visualize a sample in a transmission electron microscope the sample must (a) be thin enough such that a beam of electrons can penetrate it (<250nm, ideally <100nm), (b) be deposited onto an EM grid, which is a thin circular copper grid that is 3mm in diameter, and (c)withstand high vacuum and electron radiation within the microscope column. For tissue, samples are prepared by cutting thin sections (sectioning). For aqueous suspensions of macromolecules, including 2D crystals and ordered helical arrays, 1-5 microliters of the solution is pipetted onto the EM grid, which is then subjected to either negative staining, plunge freezing, or a combination of these sample preservation techniques, cryo-negative staining.

Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 1326 Oct 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"
Return to Cryo EM web page at http://www.nysbc.org/facilities/CEM

Principles & Protocols

Principles - Electron crystallography

Jump to Protocol

In order to visualize a sample in a transmission electron microscope the sample must (a) be thin enough such that a beam of electrons can penetrate it (<250nm, ideally <100nm), (b) be deposited onto an EM grid, which is a thin circular copper grid that is 3mm in diameter, and (c)withstand high vacuum and electron radiation within the microscope column. For tissue, samples are prepared by cutting thin sections

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<		 (sectioning). For aqueous suspensions of macromolecules, including
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>		 (sectioning). For aqueous suspensions of macromolecules, including
  2D crystals and ordered helical arrays, 1-5 microliters of the solution is pipetted onto the EM grid, which is then subjected to either
Changed:
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<		 negative staining, plunge freezing, or a combination of these sample preservation techniques,
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>		 negative staining, plunge freezing, or a combination of these sample preservation techniques, cryo-negative staining.
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<		 cryo-negative staining.
 Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 1213 Oct 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"
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>		Return to Cryo EM web page at http://www.nysbc.org/facilities/CEM
 

Principles & Protocols

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Principles - Electron crystallography

Jump to Protocol

 
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<
<

Electron crystallography

 In order to visualize a sample in a transmission electron microscope the sample must (a) be thin enough such that a beam of electrons can penetrate it (<250nm, ideally <100nm), (b) be deposited onto an EM grid, which is a thin circular copper grid that is 3mm in diameter, and (c)withstand high vacuum and electron radiation within the microscope column. For tissue, samples are prepared by cutting thin sections (sectioning). For aqueous suspensions of macromolecules, including 2D crystals and ordered helical arrays, 1-5 microliters of the solution is pipetted onto the EM grid, which is then subjected to either negative staining, plunge freezing, or a combination of these sample preservation techniques, cryo-negative staining.

Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 1103 Sep 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"

Principles & Protocols

Electron crystallography

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>
>		In order to visualize a sample in a transmission electron microscope the sample must (a) be thin enough such that a beam of electrons can penetrate it (<250nm, ideally <100nm), (b) be deposited onto an EM grid, which is a thin circular copper grid that is 3mm in diameter, and (c)withstand high vacuum and electron radiation within the microscope column. For tissue, samples are prepared by cutting thin sections (sectioning). For aqueous suspensions of macromolecules, including 2D crystals and ordered helical arrays, 1-5 microliters of the solution is pipetted onto the EM grid, which is then subjected to either negative staining, plunge freezing, or a combination of these sample preservation techniques, cryo-negative staining.
 Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 1020 Aug 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"
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Principles & Protocols

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Electron crystallography

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Electron crystallography

 Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 920 Aug 2009 - Main.KdDerr

 
META TOPICPARENT name="CemProtoc"
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Principles & Protocols

 
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Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
CEMfac Home? CEM Introduction Microscope Schedule NYSBC Directory Cryo-EM public website
 

Electron crystallography

Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 810 Aug 2009 - Main.BillRice

 
META TOPICPARENT name="CemProtoc"
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<		 NYSBC|Cryo-EM P&P: Electron crystallography
 
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Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
CEMfac Home? CEM Introduction Microscope Schedule NYSBC Directory Cryo-EM public website
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<		 Electron crystallography

Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.
Background

Protocols
Protocols

 
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Electron crystallography

Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.

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<		Protocols
Protocols
Text

 
Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 707 Apr 2009 - Main.RubenDiaz

 
META TOPICPARENT name="CemProtoc"
NYSBC|Cryo-EM P&P: Electron crystallography

Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
CEMfac Home? CEM Introduction Microscope Schedule NYSBC Directory Cryo-EM public website

Electron crystallography

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>		Two dimensional crystals are commonly formed by membrane proteins, such as bacteriorhodopsin or aquaporins. These crystals ideally consist of a single layer of molecules that are held together by specific contacts, showing crystalling order.
 Background

Protocols
Protocols

Principles
Background
Text

Protocols
Protocols
Text

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 612 Feb 2009 - Main.KakoliMitra

 
META TOPICPARENT name="CemProtoc"
NYSBC|Cryo-EM P&P: Electron crystallography

Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
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<
<
CEMfac Home NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website
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CEMfac Home? CEM Introduction Microscope Schedule NYSBC Directory Cryo-EM public website
 

Electron crystallography

Principles
Background

Protocols
Protocols

Principles
Background
Text

Protocols
Protocols
Text

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 512 Feb 2009 - Main.KakoliMitra

 
META TOPICPARENT name="CemProtoc"
NYSBC|Cryo-EM P&P: Electron crystallography

Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
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<
<
CEMfac Home NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website
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CEMfac Home NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website
 

Electron crystallography

Principles
Background

Protocols
Protocols

Principles
Background
Text

Protocols
Protocols
Text

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 412 Feb 2009 - Main.KakoliMitra

 
META TOPICPARENT name="CemProtoc"
NYSBC|Cryo-EM P&P: Electron crystallography

Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
Changed:
<
<
CEMfac Home? NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website
>
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CEMfac Home NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website
 

Electron crystallography

Principles
Background

Protocols
Protocols

Principles
Background
Text

Protocols
Protocols
Text

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 312 Feb 2009 - Main.KakoliMitra

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META TOPICPARENT name="CemProtoc"
NYSBC|Cryo-EM P&P: Electron crystallography

Principles & Protocols
Interested in EM? Using CEMfac? Principles & Protocols CEMfac Equipment Seminars & Courses
CEMfac Home? NYSBC & Cryo-EM Information? Microscope Schedule NYSBC Directory Cryo-EM public website

Electron crystallography

Principles
Background

Protocols
Protocols

Principles
Background
Text

Protocols
Protocols
Text

Public website mirror

-- KakoliMitra - 11 Feb 2009

Revision 212 Feb 2009 - Main.KakoliMitra

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Revision 111 Feb 2009 - Main.KakoliMitra

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