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Proplex screen ht 96

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The Proplex screen HT-96 is a high-throughput screening device used for protein crystallization experiments. It features a 96-well format and is designed to facilitate the rapid evaluation of multiple crystallization conditions simultaneously.

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Lab products found in correlation

Crystal screen ht, by Hampton Research (5 mentions) Wizard precipitant synergy block no 2, by Molecular Dimensions (4 mentions) Rock imager, by Formulatrix (3 mentions) Nt8 drop setter, by Formulatrix (3 mentions) Additive screen, by Hampton Research (1 mentions) Wizard precipitant synergy block 2, by Molecular Dimensions (1 mentions)

5 protocols using proplex screen ht 96

1

Crystallization of 426c core-VRC01 Antibody

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Crystallization conditions for the 426c core†-VRC01GL were screened using a Mosquito (ttplabtech)-dispensing robot. Screening was done with Rigaku Wizard Precipitant Synergy block no. 2, Molecular Dimensions Proplex screen HT-96, and Hampton Research Crystal Screen HT using the vapor diffusion method. Initial crystals were further optimized with Hampton Research Additive Screen to grow large and well-diffracting crystals. Final crystals were grown in a solution of 0.09M MgCl2, 0.09M Na-Citrate pH 5.0, 13.5% PEG 4000, 0.1M LiCl2. Crystals were cryoprotected in solutions containing 30% molar excess of their original reagents and 20% glycerol. Crystals diffracted to 2.3 Å. Data was collected at ALS 5.0.2 and processed using HKL2000 (Otwinowski and Minor, 1997 (link)).
Borst A.J., Weidle C.E., Gray M.D., Frenz B., Snijder J., Joyce M.G., Georgiev I.S., Stewart-Jones G.B., Kwong P.D., McGuire A.T., DiMaio F., Stamatatos L., Pancera M, & Veesler D. (2018). Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core. eLife, 7, e37688.
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2

Optimizing Protein-Ligand Crystal Structures

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Crystallization conditions were screened and monitored with an NT8 drop setter and Rock Imager (Formulatrix). Screening was done with Rigaku Wizard Precipitant Synergy block no. 2 (MD15-PS-B), Molecular Dimensions Proplex screen HT-96 (MD1–38), and Hampton Research Crystal Screen HT (HR2–130) using the sitting drop vapor diffusion method. P-p1f1fab + eOD-GT8 crystals were further optimized with hanging drop trays using vapor diffusion method. Final crystals for P-p1f1fab + eODGT8 were grown in 22.5% PEG 3350, 13.5% Isopropanol, 0.18M Ammonium Citrate pH 4.0. Final crystals for P-p3b3fab + 426c Core were grown in 0.67% PEG 4000, 0.67M Ammonium Citrate pH 5.5. P-p1f1fab + eODGT8 crystal were cryo protected in a solution of 20% molar excess of the crystallization condition and 20% Ethylene Glycol. P-p3b3fab + 426c Core were cryoprotected in the original crystallization condition. P-p3b3fab + 426c Core and P-p1f1fab + eODGT8 were sent to ALS 5.0.2 and diffraction data was collected to 3.59 Å and 3.2 Å respectively. Data were processed using HKL2000 (Otwinowski and Minor, 1997 ).
Parks K.R., MacCamy A.J., Trichka J., Gray M., Weidle C., Borst A.J., Khechaduri A., Takushi B., Agrawal P., Guenaga J., Wyatt R.T., Coler R., Seaman M., LaBranche C., Montefiori D.C., Veesler D., Pancera M., McGuire A, & Stamatatos L. (2019). Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell reports, 29(10), 3060-3072.e7.
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3

Crystallization and Structure Determination of Protein

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Crystallization conditions were screened and monitored with an NT8 drop setter and Rock Imager (Formulatrix). Screening was done with Rigaku Wizard Precipitant Synergy block no. 2, Molecular Dimensions Proplex screen HT-96, and Hampton Research Crystal Screen HT using the sitting drop vapor diffusion method. Final crystals were grown in a solution of 18.43% PEG 3350, 11- .01%, Lithium Sulfate, 0.11 M Imidazole pH 6.5. Crystals were cryoprotected in a solution of 30% excess of the crystallization condition and 20% glycerol. Crystals were sent to ALS 5.0.1 and diffraction data was collected to 3.42 Å. Data was processed using HKL-2000 (Otwinowski and Minor, 1997 ). The structure was solved using molecular replacement using PDB ID: 5IFA as a search model in Phaser in Phenix (Adams et al., 2010 (link)). The structure was further refined with COOT (Emsley and Cowtan, 2004 (link)) and Phenix (Adams et al., 2010 (link)). The refinement statistics are summarized in Supplemental Table 2.
Lin Y.R., Rachael Parks K., Weidle C., Naidu A.S., Khechaduri A., Riker A.O., Takushi B., Chun J.H., Borst A.J., Veesler D., Stuart A., Agrawal P., Gray M., Pancera M., Huang P.S, & Stamatatos L. (2020). HIV-1 VRC01 germline-targeting immunogens select distinct epitope-specific B cell receptors. Immunity, 53(4), 840-851.e6.
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4

Optimizing Protein-Ligand Crystal Structures

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Crystallization conditions were screened and monitored with an NT8 drop setter and Rock Imager (Formulatrix). Screening was done with Rigaku Wizard Precipitant Synergy block no. 2 (MD15-PS-B), Molecular Dimensions Proplex screen HT-96 (MD1–38), and Hampton Research Crystal Screen HT (HR2–130) using the sitting drop vapor diffusion method. P-p1f1fab + eOD-GT8 crystals were further optimized with hanging drop trays using vapor diffusion method. Final crystals for P-p1f1fab + eODGT8 were grown in 22.5% PEG 3350, 13.5% Isopropanol, 0.18M Ammonium Citrate pH 4.0. Final crystals for P-p3b3fab + 426c Core were grown in 0.67% PEG 4000, 0.67M Ammonium Citrate pH 5.5. P-p1f1fab + eODGT8 crystal were cryo protected in a solution of 20% molar excess of the crystallization condition and 20% Ethylene Glycol. P-p3b3fab + 426c Core were cryoprotected in the original crystallization condition. P-p3b3fab + 426c Core and P-p1f1fab + eODGT8 were sent to ALS 5.0.2 and diffraction data was collected to 3.59 Å and 3.2 Å respectively. Data were processed using HKL2000 (Otwinowski and Minor, 1997 ).
Parks K.R., MacCamy A.J., Trichka J., Gray M., Weidle C., Borst A.J., Khechaduri A., Takushi B., Agrawal P., Guenaga J., Wyatt R.T., Coler R., Seaman M., LaBranche C., Montefiori D.C., Veesler D., Pancera M., McGuire A, & Stamatatos L. (2019). Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell reports, 29(10), 3060-3072.e7.
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5

Obtaining High-Resolution Crystals of AMMO1 Fab

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Crystals of AMMO1 Fab were obtained using a NT8 dispensing robot and screening was done with Rigaku Wizard Precipitant Synergy block#2, Molecular Dimensions Proplex screen HT-96, Hampton Research Crystal Screen HT by the vapor diffusion method. Crystals used for diffraction data were grown in 16.75% PEG 400, 13.4% PEG 3350, 0.1M MgCl2, 0.1M Tris pH 8.5. Crystals were cryo-protected in solutions containing 30% molar excess of their original reagents and 20% Glycerol. Crystal diffracted to 1.6 Å (See Table S4). Data was collected at ALS 5.1 and 5.2 and processed using HKL2000 (Otwinowski and Minor, 1997 ).
Snijder J., Ortego M.S., Weidle C., Stuart A.B., Gray M.D., McElrath M.J., Pancera M., Veesler D, & McGuire A.T. (2018). An antibody targeting the fusion machinery neutralizes dual-tropic infection and defines a site of vulnerability on Epstein-Barr virus. Immunity, 48(4), 799-811.e9.
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