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Merck & Co hcas ii
Hcas Ii, supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hcas+ii/hcas2/10__1039_slash_d4md01018c-138-28-36
Average 90 stars, based on 1 article reviews
hcas ii - by Bioz Stars, 2026-10
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Related Articles

Inhibition:

Article Title: X-ray crystallographic and kinetic studies of biguanide containing aryl sulfonamides as Carbonic anhydrase inhibitors
Article Snippet: The inhibition constants were obtained by nonlinear leastsquares methods using PRISM 3 and the Cheng−Prusoff equation as reported earlier39 and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while other isoenzymes were obtained in-house.40 Expression and purification of the hCA XII mimic To generate the hCA XII mimic,33 the CA II gene was used as the template, and nine specific mutations were introduced to reproduce key features of the hCA XII active site.

Article Title: Lasamide Containing Sulfonylpiperazines as Effective Agents for the Management of Glaucoma Associated Symptoms
Article Snippet: The inhibition constants were obtained by non‐linear least‐squares methods using PRISM 3 and the Cheng‐Prusoff equation as reported earlier and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while hCAs IX and XII are recombinant and obtained in‐house .

Expressing:

Article Title: X-ray crystallographic and kinetic studies of biguanide containing aryl sulfonamides as Carbonic anhydrase inhibitors
Article Snippet: The inhibition constants were obtained by nonlinear leastsquares methods using PRISM 3 and the Cheng−Prusoff equation as reported earlier39 and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while other isoenzymes were obtained in-house.40 Expression and purification of the hCA XII mimic To generate the hCA XII mimic,33 the CA II gene was used as the template, and nine specific mutations were introduced to reproduce key features of the hCA XII active site.

Article Title: Lasamide Containing Sulfonylpiperazines as Effective Agents for the Management of Glaucoma Associated Symptoms
Article Snippet: The inhibition constants were obtained by non‐linear least‐squares methods using PRISM 3 and the Cheng‐Prusoff equation as reported earlier and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while hCAs IX and XII are recombinant and obtained in‐house .

Purification:

Article Title: X-ray crystallographic and kinetic studies of biguanide containing aryl sulfonamides as Carbonic anhydrase inhibitors
Article Snippet: The inhibition constants were obtained by nonlinear leastsquares methods using PRISM 3 and the Cheng−Prusoff equation as reported earlier39 and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while other isoenzymes were obtained in-house.40 Expression and purification of the hCA XII mimic To generate the hCA XII mimic,33 the CA II gene was used as the template, and nine specific mutations were introduced to reproduce key features of the hCA XII active site.

Article Title: Lasamide Containing Sulfonylpiperazines as Effective Agents for the Management of Glaucoma Associated Symptoms
Article Snippet: The inhibition constants were obtained by non‐linear least‐squares methods using PRISM 3 and the Cheng‐Prusoff equation as reported earlier and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while hCAs IX and XII are recombinant and obtained in‐house .

Recombinant:

Article Title: X-ray crystallographic and kinetic studies of biguanide containing aryl sulfonamides as Carbonic anhydrase inhibitors
Article Snippet: The inhibition constants were obtained by nonlinear leastsquares methods using PRISM 3 and the Cheng−Prusoff equation as reported earlier39 and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while other isoenzymes were obtained in-house.40 Expression and purification of the hCA XII mimic To generate the hCA XII mimic,33 the CA II gene was used as the template, and nine specific mutations were introduced to reproduce key features of the hCA XII active site.

Article Title: Lasamide Containing Sulfonylpiperazines as Effective Agents for the Management of Glaucoma Associated Symptoms
Article Snippet: The inhibition constants were obtained by non‐linear least‐squares methods using PRISM 3 and the Cheng‐Prusoff equation as reported earlier and represent the mean from at least three different determinations. hCAs I and II were purchased from Merck, while hCAs IX and XII are recombinant and obtained in‐house .



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Changsheng Bio Technology Co recombinant hca ii
Recombinant Hca Ii, supplied by Changsheng Bio Technology Co, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hca ii  (JEOL)
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Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
Pcr Array Hca Ii, supplied by Real Time Primers, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Merck & Co hcas ii
Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
Hcas Ii, supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/hcas+ii/hcas2/10__1039_slash_d4md01018c-138-28-36
Average 90 stars, based on 1 article reviews
hcas ii - by Bioz Stars, 2026-10
90/100 stars
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Image Search Results


Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and HCA II:AZM MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .

Journal: Acta Crystallographica Section D: Structural Biology

Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

doi: 10.1107/S205979832500912X

Figure Lengend Snippet: Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and HCA II:AZM MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .

Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

Techniques: Microscopy

Site-specific damage of aspartic and glutamic acids in the HCA II:AZM protein complex. The 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. The mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3.0σ above and below the mean. A section covering 2 Å around atoms is shown for all densities. The electron doses are as specified in the figure.

Journal: Acta Crystallographica Section D: Structural Biology

Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

doi: 10.1107/S205979832500912X

Figure Lengend Snippet: Site-specific damage of aspartic and glutamic acids in the HCA II:AZM protein complex. The 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. The mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3.0σ above and below the mean. A section covering 2 Å around atoms is shown for all densities. The electron doses are as specified in the figure.

Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

Techniques:

How radiation damage affects the quality of protein–ligand binding properties. ( a ) Polar contacts between HCA II and its inhibitor AZM. ( b ) The quality of the density maps around the HCA II:AZM complex and zinc atomic B factors. 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3σ above and below the mean. The 1-10F (6.75 MGy) structure shows some signs of incompleteness, while the 21-35F and All F structures exhibit signs of radiation damage as judged from 2 mF o − DF c maps and increased mF o − DF c features. The 1-20F data set is more complete with low signs of radiation damage and has the lowest isotropic B factor for the active-site zinc metal. The electron doses are as specified in the figure.

Journal: Acta Crystallographica Section D: Structural Biology

Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

doi: 10.1107/S205979832500912X

Figure Lengend Snippet: How radiation damage affects the quality of protein–ligand binding properties. ( a ) Polar contacts between HCA II and its inhibitor AZM. ( b ) The quality of the density maps around the HCA II:AZM complex and zinc atomic B factors. 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3σ above and below the mean. The 1-10F (6.75 MGy) structure shows some signs of incompleteness, while the 21-35F and All F structures exhibit signs of radiation damage as judged from 2 mF o − DF c maps and increased mF o − DF c features. The 1-20F data set is more complete with low signs of radiation damage and has the lowest isotropic B factor for the active-site zinc metal. The electron doses are as specified in the figure.

Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

Techniques: Ligand Binding Assay