Optimizing performance in cross-linking negative-tone molecular resists

2015 ◽  
Author(s):  
Richard A. Lawson ◽  
Hannah Narcross ◽  
Brandon Sharp ◽  
Jun Sung Chun ◽  
Mark Neisser ◽  
...  
Keyword(s):  
Cross Linking ◽  
Negative Tone

Methods of controlling cross-linking in negative-tone resists

2014 ◽  
Author(s):  
Richard A. Lawson ◽  
Jun Sung Chun ◽  
Mark Neisser ◽  
Laren M. Tolbert ◽  
Clifford L. Henderson
Keyword(s):  
Cross Linking ◽  
Negative Tone

FTIR SPECTROSCOPIC STUDIES ON CROSS LINKING OF SU-8 PHOTORESIST

COSMOS ◽  
2013 ◽  
Vol 09 (01) ◽  
pp. 37-46 ◽  
Author(s):  
S. M. P. KALAISELVI ◽  
T. L. TAN ◽  
R. S. RAWAT ◽  
P. LEE ◽  
S. P. HEUSSLER ◽  
...  
Keyword(s):  
Process Parameters ◽  
Spectroscopic Studies ◽  
Exposure Dose ◽  
Good Evidence ◽  
Pattern Generation ◽  
Cross Linking ◽  
X Ray ◽  
Dosage Requirement ◽  
Negative Tone ◽  
Micro Structures

The usage of chemically-amplified, negative tone SU-8 photoresist is numerous, spanning industrial, scientific and medical fields. Hence, in this study, some preliminary studies were conducted to understand the dosage and heat treatment requirements of the SU-8 photoresist essential for pattern generation using X-ray lithography. In this work, using Synchrotron as the X-ray source, SU-8 photoresist was characterized for X-ray lithography in terms of its process parameters such as X-ray exposure dose, post exposure bake (PEB) time and temperature for various photoresist thicknesses which is considered worthwhile in view of applications of SU-8 for the fabrication of very high aspect ratio micro structures. The process parameters were varied and the resultant cross linking of the molecular chains of the photoresist was accurately monitored using a Fourier Transform Infra-Red (FTIR) spectrometer and the results are discussed. The infrared absorption peak at 914 cm-1 in the spectrum of the SU-8 photoresist was found to be a useful indicator for the completion of cross linking in the SU-8 photoresist. Results show that the cross linking of the SU-8 photoresist is at a higher rate from 0 J/cm3 to 30 J/cm3 after which the peak almost saturates regardless of the PEB time. It is a good evidence for the validation of dosage requirement of SU-8 photoresist for effective completion of cross linking, which in turn is a requirement for efficient fabrication of micro and nano structures. An analogous behavior was also observed between the extent of cross linking and the PEB time and temperature. The rate of cross linking declines after a certain period of PEB time regardless of PEB temperature. The obtained results also show a definite relation between variation of the absorbance area of the peak at 914 cm-1 and the X-ray exposure dose.

Base developable negative tone molecular resist based on epoxide cross-linking

2015 ◽  
Author(s):  
Brandon Sharp ◽  
Richard A. Lawson ◽  
Ashten Fralick ◽  
Hannah Narcross ◽  
Jun Sung Chun ◽  
...  
Keyword(s):  
Cross Linking ◽  
Negative Tone

Wet Chemical Processing with Megasonics Assist for the Removal of Bumping Process Photomasks

2014 ◽  
Vol 2014 (DPC) ◽  
pp. 001966-001981 ◽  
Author(s):  
Sohn Hong Seong ◽  
John Tracy
Keyword(s):  
Chain Scission ◽  
Cross Linking ◽  
Solvent Exposure ◽  
Major Drawback ◽  
Photoresist Layer ◽  
Advanced Packaging ◽  
Thick Photoresist ◽  
Negative Tone ◽  
Chemical Events ◽  
New Generation

A new generation of negative tone resists by TOK, JSR, and Dow Chemical is gaining momentum in advanced packaging applications. Resist thickness requirements are actually increasing to the 50-100 um range as Cu pillars are adopted to accommodate the tighter pitches required in advanced packaging. In order to form pillars the resist must be thicker to contain the entire bump structure. Thick, negative tone resists are more transparent to exposure light wavelengths than positive tone resists and can be exposed by the lithography process much faster (~1 x 104 cross-linking chemical events are driven by 1 photochemical event vs. 100 – 1000 for positive tone resist).1 Therefore exposure times can be shorter, post-exposure bake steps can be shorter, and delay before or after exposure is not necessary, saving photolithography time and CoO. And, due to more complete cross-linking throughout the resist, the resist mask profiles are truer (from Flack et.al, “A Comparison of New Thick Photoresists for Solder Bumping”, SPIE 2005).1 The major drawback to negative tone resists is that the solvent strip times of the highly cross-linked resist masks are much longer than for positive tone. Flack et.al. noted resist strip times of 5 minutes for two positive resists used in their experiments vs. 50 minutes for the AZ-100nXT negative tone resist, using AZ400T at 80°C (most likely in an immersion tool). Long strip times or special stripping requirements are noted on the data sheets of the other majority suppliers of negative resists as well. Akrion engineers have developed a novel, single-wafer, negative PR strip processes using organic solvents plus Goldfinger megasonics, to provide 30 - 70% reductions in process times and the associated chemical consumption when compared to processes that do not utilize a megasonics assist. The multi-step process can be accomplished in a single process chamber, with each step optimized for time and temperature based on the resist thickness and solvent stripping chemistry used. In the Akrion process, a period of solvent exposure at low wafer spin speed is used initially to begin swelling and dissolving the thick photoresist layer. This is followed by a second solvent exposure step using aggressive frontside megasonic energy to promote polymer chain scission throughout the bulk of the photoresist layer. Following this step A DI water rinse and spin dry step are sufficient to completely remove the solvent, dissolved photoresist and any polymer residues. This paper reviews the development of the Akrion process and several examples of improvement in stripping time and results from work with customers.

Influence of Calcium Ions on the Plant Cell Surface: Membrane Fusions and Conformational Changes

1974 ◽  
Vol 32 ◽  
pp. 154-155
Author(s):  
D. James Morré ◽  
Charles E. Bracker ◽  
William J. VanDerWoude
Keyword(s):  
Cell Wall ◽  
Cell Surface ◽  
Conformational Changes ◽  
Calcium Ions ◽  
Surface Membrane ◽  
Carboxyl Groups ◽  
Cross Linking ◽  
Ultrastructural Evidence ◽  
Glycine Max L ◽  
Wall Extensibility

Calcium ions in the concentration range 5-100 mM inhibit auxin-induced cell elongation and wall extensibility of plant stems. Inhibition of wall extensibility requires that the tissue be living; growth inhibition cannot be explained on the basis of cross-linking of carboxyl groups of cell wall uronides by calcium ions. In this study, ultrastructural evidence was sought for an interaction of calcium ions with some component other than the wall at the cell surface of soybean (Glycine max (L.) Merr.) hypocotyls.

Embedding Procedure for Water Swollen Samples

1970 ◽  
Vol 28 ◽  
pp. 504-505
Author(s):  
Ann M. Thomas ◽  
Virginia Shemeley
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Ion Exchange ◽  
Structural Changes ◽  
Cross Linking ◽  
Ion Exchange Resins ◽  
Transmission Electron ◽  
First Pass ◽  
Exchange Resins

Those samples which swell rapidly when exposed to water are, at best, difficult to section for transmission electron microscopy. Some materials literally burst out of the embedding block with the first pass by the knife, and even the most rapid cutting cycle produces sections of limited value. Many ion exchange resins swell in water; some undergo irreversible structural changes when dried. We developed our embedding procedure to handle this type of sample, but it should be applicable to many materials that present similar sectioning difficulties.The purpose of our embedding procedure is to build up a cross-linking network throughout the sample, while it is in a water swollen state. Our procedure was suggested to us by the work of Rosenberg, where he mentioned the formation of a tridimensional structure by the polymerization of the GMA biproduct, triglycol dimethacrylate.

The Current Situation in Chemical Stabilization of Biological Materials

1972 ◽  
Vol 30 ◽  
pp. 132-133
Author(s):  
John H. Luft
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Osmium Tetroxide ◽  
Molecular Level ◽  
Cross Linking ◽  
Chemical Stabilization ◽  
Specimen Preparation ◽  
Sufficient Condition ◽  
Radio Telescopes

With information processing devices such as radio telescopes, microscopes or hi-fi systems, the quality of the output often is limited by distortion or noise introduced at the input stage of the device. This analogy can be extended usefully to specimen preparation for the electron microscope; fixation, which initiates the processing sequence, is the single most important step and, unfortunately, is the least well understood. Although there is an abundance of fixation mixtures recommended in the light microscopy literature, osmium tetroxide and glutaraldehyde are favored for electron microscopy. These fixatives react vigorously with proteins at the molecular level. There is clear evidence for the cross-linking of proteins both by osmium tetroxide and glutaraldehyde and cross-linking may be a necessary if not sufficient condition to define fixatives as a class.

Parathyroid gland before and after cisplatin treatment

1987 ◽  
Vol 45 ◽  
pp. 860-861
Author(s):  
S.K. Aggarwal ◽  
J.M. Fadool
Keyword(s):  
Parathyroid Gland ◽  
Wistar Rats ◽  
Antitumor Agent ◽  
The Body ◽  
Cross Linking ◽  
Limiting Factor ◽  
Hormonal Changes ◽  
Primary Mechanism ◽  
Before And After ◽  
Dna Strands

Cisplatin (CDDP) a potent antitumor agent suffers from severe toxic side effects with nephrotoxicity being the major dose-limiting factor, The primary mechanism of its action has been proposed to be through its cross-linking DNA strands. It has also been shown to inactivate various transport enzymes and induce hypocalcemia and hypomagnesemia that may be the underlying cause for some of its toxicities. The present is an effort to study its influence on the parathyroid gland for any hormonal changes that control calcium levels in the body.Male Swiss Wistar rats (Crl: (WI) BR) weighing 200-300 g and of 60 days in age were injected (ip) with cisplatin (7mg/kg in normal saline). The controls received saline injections only. The animals were injected (iv) with calcium (0.5 ml of 10% calcium gluconate/day) and were killed by decapitation on day 1 through 5. Trunk blood was collected in heparinized tubes.

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

CRYO-Electron Microscopy of the Acto-Myosin-ATP Complex

1990 ◽  
Vol 48 (1) ◽  
pp. 248-249
Author(s):  
John Trinickt ◽  
Howard White
Keyword(s):  
Electron Microscopy ◽  
Atp Hydrolysis ◽  
Myosin Head ◽  
Bound State ◽  
Cross Linking ◽  
Weakly Bound ◽  
Cryo Electron Microscopy ◽  
Myosin Subfragment 1 ◽  
Attached State ◽  
High Fraction

The primary force of muscle contraction is thought to involve a change in the myosin head whilst attached to actin, the energy coming from ATP hydrolysis. This change in attached state could either be a conformational change in the head or an alteration in the binding angle made with actin. A considerable amount is known about one bound state, the so-called strongly attached state, which occurs in the presence of ADP or in the absence of nucleotide. In this state, which probably corresponds to the last attached state of the force-producing cycle, the angle between the long axis myosin head and the actin filament is roughly 45°. Details of other attached states before and during power production have been difficult to obtain because, even at very high protein concentration, the complex is almost completely dissociated by ATP. Electron micrographs of the complex in the presence of ATP have therefore been obtained only after chemically cross-linking myosin subfragment-1 (S1) to actin filaments to prevent dissociation. But it is unclear then whether the variability in attachment angle observed is due merely to the cross-link acting as a hinge.We have recently found low ionic-strength conditions under which, without resorting to cross-linking, a high fraction of S1 is bound to actin during steady state ATP hydrolysis. The structure of this complex is being studied by cryo-electron microscopy of hydrated specimens. Most advantages of frozen specimens over ambient temperature methods such as negative staining have already been documented. These include improved preservation and fixation rates and the ability to observe protein directly rather than a surrounding stain envelope. In the present experiments, hydrated specimens have the additional benefit that it is feasible to use protein concentrations roughly two orders of magnitude higher than in conventional specimens, thereby reducing dissociation of weakly bound complexes.

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