From 78a29c41414463d8c7768dd1cd09179a7af05149 Mon Sep 17 00:00:00 2001 From: Mojca Lorber Date: Mon, 11 Feb 2019 16:15:56 +0100 Subject: [PATCH] add templates after protocol_keyword_team rake task was run --- .../templates/experiment_422/experiment.json | 2 +- .../templates/experiment_423/experiment.json | 2 +- .../experiment_430/assets/2838/Example.png | Bin 159276 -> 0 bytes .../experiment_430/assets/3096/Example.png | Bin 119847 -> 0 bytes .../assets/3097/Streaking_bacteria_method.png | Bin 100610 -> 0 bytes .../templates/experiment_430/experiment.json | 2 +- .../templates/experiment_433/experiment.json | 2 +- .../templates/experiment_436/experiment.json | 2 +- .../templates/experiment_440/experiment.json | 2 +- .../templates/experiment_454/experiment.json | 2 +- .../templates/experiment_497/experiment.json | 2 +- 11 files changed, 8 insertions(+), 8 deletions(-) delete mode 100644 app/assets/templates/experiment_430/assets/2838/Example.png delete mode 100644 app/assets/templates/experiment_430/assets/3096/Example.png delete mode 100644 app/assets/templates/experiment_430/assets/3097/Streaking_bacteria_method.png diff --git a/app/assets/templates/experiment_422/experiment.json b/app/assets/templates/experiment_422/experiment.json index 39d146a5c..49fb8f5b3 100644 --- a/app/assets/templates/experiment_422/experiment.json +++ b/app/assets/templates/experiment_422/experiment.json @@ -1 +1 @@ -{"experiment":{"id":422,"name":"CRISPR transformations with Agrobacterium tumefaciens","description":"The clustered regularly interspaced short palindromic repeats(CRISPR) associated Cas9/sgRNA system is a novel targeted genome-editing technique derived from the bacterial immune system. 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Ensure no air is trapped under the column net. Close column outlet leaving 1–2 cm of the buffer in the column.","checked":false,"checklist_id":968,"created_at":"2018-12-21T13:27:09.421Z","updated_at":"2018-12-21T13:27:09.421Z","created_by_id":null,"last_modified_by_id":null,"position":1},{"id":3986,"text":"Gently resuspend the medium. For media not supplied in suspension, use a medium: buffer ratio of approximately 1:2 to produce a suspension for mixing during rehydration. Avoid using magnetic stirrers since they may damage the matrix.","checked":false,"checklist_id":968,"created_at":"2018-12-21T13:27:09.427Z","updated_at":"2018-12-21T13:27:09.427Z","created_by_id":null,"last_modified_by_id":null,"position":2}]}],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":4279,"name":"Stop the pump and close the column outlet.","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp style=\"text-align: justify;\"\u003eRemove the top piece and carefully fill the rest of the column with buffer to form an upward meniscus at the top. Insert the adaptor into the column at an angle, ensuring that no air is trapped under the net. Slide the adaptor slowly down the column (the outlet of the adaptor should be open) until the mark is reached. Lock the adaptor in position. Connect the column to the pump and begin equilibration. Re-position the adaptor if necessary.\u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":2,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-11-08T10:28:49.069Z","updated_at":"2018-12-21T13:29:08.411Z","last_modified_by_id":202,"protocol_id":3405},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":4283,"name":"Column fill and setting the column outlet.","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp style=\"text-align: justify;\"\u003eEstimate the amount of resuspended medium required and our the required volume of the medium into the column. 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Always operate the centrifuge with all buckets in place, even if two opposing buckets are empty.","checked":false,"checklist_id":934,"created_at":"2018-12-18T14:10:46.354Z","updated_at":"2018-12-18T14:10:46.354Z","created_by_id":null,"last_modified_by_id":null,"position":4}]}],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":4273,"name":"Buffer exchange and desalting","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp\u003e\u003cstrong\u003eFill the syringe with buffer.\u003c/strong\u003e To avoid introducing air into the column, connect the column \"drop to drop\" to the syringe (via the adapter). Wash the column. Use 25 mL buffer at 5 mL/min to remove completely the 20% ethanol (supplied as storage buffer). If air is trapped in the column, wash with degassed buffer until the air disappears. Air bubbles introduced onto the column by accident during sample application do not influence the separation.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eApplying the sample.\u003c/strong\u003e Use a 2–5 mL syringe at a flow rate between 1–10 mL/min. Discard the liquid eluted from the column. If the sample volume is less than 1.5 mL, change to buffer and proceed with the injection until a total of 1.5 mL has been eluted. Discard the eluted liquid.pter). Elute the protein with the appropriate volume.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSelect volume from the table.\u003c/strong\u003e\u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":2,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-11-08T10:28:48.761Z","updated_at":"2018-12-20T13:33:54.642Z","last_modified_by_id":202,"protocol_id":3403},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[{"id":438,"step_id":4273,"table_id":554}],"tables":[{"id":554,"created_at":"2018-11-08T10:28:48.787Z","updated_at":"2018-12-20T13:33:54.646Z","created_by_id":202,"last_modified_by_id":202,"name":"","team_id":1,"contents":"eyJkYXRhIjpbWyJTYW1wbGUgbG9hZCAobUwpIiwiQWRkIGJ1ZmZlciAobUwp\nIiwiRWx1dGUgYW5kIGNvbGxlY3QgKG1MKSIsIllpZWxkICglKSIsIlJlbWFp\nbmluZyBzYWx0ICglKSIsIkRpbHV0aW9uIGZhY3RvciAoJSkiXSxbIjAsMjUi\nLCIxLDI1IiwiMSwwIiwiPjk1IiwiMCwwIiwiNCwwIl0sWyIwLDUwIiwiMSww\nIiwiMSw1IiwiPjk1IiwiPDAsMSIsIjMsMCJdLFsiMSwwMCIsIjAsNSIsIjIs\nMCIsIj45NSIsIjwwLDIiLCIyLDAiXSxbIjEsNTAiLCIwIiwiMiwwIiwiPjk1\nIiwiPDAsMiIsIjEsMyJdXX0=\n","data_vector":"JzAnOjE2LDIxLDIzLDI0LDI2LDI3LDMwLDM0LDM3LDQwLDQzLDQ1LDQ4LDUx\nLDUzLDU1ICcwMCc6MzkgJzEnOjE4LDIwLDI5LDMxLDM1LDM4LDQ5LDU3ICcy\nJzo0Miw0Niw0Nyw1Miw1NiAnMjUnOjE3LDE5ICczJzozNiw1OCAnNCc6MjUg\nJzUnOjMyLDQxICc1MCc6MjgsNTAgJzk1JzoyMiwzMyw0NCw1NCAnYWRkJzo0\nICdhbmQnOjggJ2J1ZmZlcic6NSAnY29sbGVjdCc6OSAnZGlsdXRpb24nOjE0\nICdlbHV0ZSc6NyAnZmFjdG9yJzoxNSAnbG9hZCc6MiAnbWwnOjMsNiwxMCAn\ncmVtYWluaW5nJzoxMiAnc2FsdCc6MTMgJ3NhbXBsZSc6MSAneWllbGQnOjEx\n"}]},{"step":{"id":5210,"name":"Centrifugation of samples","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp style=\"text-align: justify;\"\u003eSwitch on and follow the manufacturer's instructions to set the centrifugation conditions.\u003cbr\u003eFor small sample volumes or proteins that adsorb non-specifically to filters, centrifuge at 10 000 x g for 15 minutes. For cell lysates, centrifuge at 40 000–50 000 x g for 30 minutes. Close and lock the lid and then start the centrifuge cycle. If excessive vibration occurs, or if a crack is heard or tube breakage is suspected, switch off the unit. Open the centrifuge only after the signal for the end of centrifugation is seen. Remove the sealed buckets (not tubes) slowly and carefully to prevent re-suspension. \u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":1,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-12-18T14:12:05.603Z","updated_at":"2019-02-11T12:51:42.964Z","last_modified_by_id":1,"protocol_id":3403},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]}]}],"results":[]},{"my_module":{"id":2098,"name":"Analysis","due_date":null,"description":null,"x":105,"y":0,"my_module_group_id":1190,"created_at":"2018-11-08T10:28:49.665Z","updated_at":"2018-12-21T13:25:20.388Z","archived":false,"archived_on":null,"created_by_id":202,"last_modified_by_id":null,"archived_by_id":null,"restored_by_id":null,"restored_on":null,"nr_of_assigned_samples":0,"workflow_order":3,"experiment_id":423,"state":"uncompleted","completed_on":null,"electronic_signature_status":"unlocked","electronic_signature_status_locked_at":null},"outputs":[],"my_module_tags":[],"task_comments":[],"my_module_repository_rows":[],"user_my_modules":[],"protocols":[{"protocol":{"id":3409,"name":null,"authors":null,"description":null,"added_by_id":null,"my_module_id":2098,"team_id":1,"protocol_type":"unlinked","parent_id":null,"parent_updated_at":null,"archived_by_id":null,"archived_on":null,"restored_by_id":null,"restored_on":null,"created_at":"2018-11-08T10:28:49.719Z","updated_at":"2018-12-24T09:22:25.677Z","published_on":null,"nr_of_linked_children":0},"protocol_protocol_keywords":[],"steps":[{"step":{"id":5226,"name":"Purity analysis: SDS PAGE","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\n\u003cem\u003e\u003cstrong\u003eSodium dodecyl \u003c/strong\u003e\u003c/em\u003esulfate polyacrylamide\u003cem\u003e\u003cstrong\u003e gel electrophoresis (SDS-PAGE) is a technology commonly used in protein purification and analysis.\u003c/strong\u003e \u003cstrong\u003eSDS-PAGE can separate proteins according to the differences in the charge and the different mobility due to different molecular sizes\u003c/strong\u003e\u003c/em\u003e. If the protein sample has been highly purified and contains only one protein, the results would show a single protein band after SDS-PAGE separation. However, when there are multiple proteins in the protein samples, different proteins can be separated into multiple protein bands through SDS-PAGE. Therefore, SDS-PAGE technology provides a direct way to analyze the purity of protein samples.\u003c/body\u003e\u003c/html\u003e","position":1,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-12-19T08:41:05.893Z","updated_at":"2018-12-24T09:22:25.629Z","last_modified_by_id":202,"protocol_id":3409},"checklists":[{"checklist":{"id":970,"name":"Guideline:","step_id":5226,"created_at":"2018-12-21T13:36:26.307Z","updated_at":"2018-12-21T13:36:26.307Z","created_by_id":null,"last_modified_by_id":null},"checklist_items":[{"id":3994,"text":"Add 2 µL of 6X SDS loading buffer to 5–10 µL of supernatant from crude extracts, cell lysates or purified fractions as appropriate.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.308Z","updated_at":"2018-12-21T13:36:26.308Z","created_by_id":null,"last_modified_by_id":null,"position":0},{"id":3995,"text":"Vortex briefly and heat for 5 minutes at +90 to +100 °C.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.316Z","updated_at":"2018-12-21T13:36:26.316Z","created_by_id":null,"last_modified_by_id":null,"position":1},{"id":3996,"text":"Load the samples onto an SDS-polyacrylamide gel.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.323Z","updated_at":"2018-12-21T13:36:26.323Z","created_by_id":null,"last_modified_by_id":null,"position":2},{"id":3997,"text":"Run the gel and stain with Coomassie Blue or silver.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.329Z","updated_at":"2018-12-21T13:36:26.329Z","created_by_id":null,"last_modified_by_id":null,"position":3}]}],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":5233,"name":"Protein Identity Analysis: Mass Spectromety","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\n\u003cdiv\u003eSelect the appropriate MS Instrument. Samples are measured according to Mass Spectrometer manual. After the MS data is collected, the next step is to\u003cstrong\u003e perform a database search to identify the proteins and/or peptides analyzed by MS\u003c/strong\u003e. A number of parameters can affect the outcome of a database search, and, ultimately, search parameters should consider the history of the sample, \u003cstrong\u003esuch as organism, enzymatic or chemical digestion, and reduction/alkylation steps\u003c/strong\u003e. Differences among search engines can include the scoring algorithm, whether it considers data quality, and whether it considers all fragment ion types or only a subset. 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justify;\"\u003e \u003c/div\u003e\n\u003c/body\u003e\u003c/html\u003e","position":2,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-12-19T09:32:37.616Z","updated_at":"2018-12-21T13:38:06.144Z","last_modified_by_id":202,"protocol_id":3409},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[{"id":539,"step_id":5233,"table_id":676}],"tables":[{"id":676,"created_at":"2018-12-19T09:32:37.619Z","updated_at":"2018-12-21T13:38:06.147Z","created_by_id":202,"last_modified_by_id":202,"name":"Commonly used mass spectrometers and their 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analysis: Bradford Assay","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp\u003eFollow guidelines below to perform a Bradford assay. \u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":0,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-11-19T08:02:56.820Z","updated_at":"2018-12-24T09:20:53.287Z","last_modified_by_id":202,"protocol_id":3409},"checklists":[{"checklist":{"id":969,"name":"Guideline:","step_id":4643,"created_at":"2018-12-21T13:35:09.660Z","updated_at":"2018-12-21T13:35:09.660Z","created_by_id":null,"last_modified_by_id":null},"checklist_items":[{"id":3987,"text":"Prepare five to eight dilutions of BSA standard with a range of 5 to 100 µg protein.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.662Z","updated_at":"2018-12-21T13:35:09.662Z","created_by_id":null,"last_modified_by_id":null,"position":0},{"id":3988,"text":"Dilute protein samples to obtain 5-100 µg protein/30 µL.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.669Z","updated_at":"2018-12-21T13:35:09.669Z","created_by_id":null,"last_modified_by_id":null,"position":1},{"id":3989,"text":"Set two blank tubes. For the standard curve, add 30 µL of water instead of the standard solution. For the unknown protein samples, add 30 µL protein preparation buffer instead. Protein solutions are normally assayed in duplicate or triplicate.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.675Z","updated_at":"2018-12-21T13:35:09.675Z","created_by_id":null,"last_modified_by_id":null,"position":2},{"id":3990,"text":"Add 1.5 mL of Bradford reagent to each tube and mix well.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.682Z","updated_at":"2018-12-21T13:35:09.682Z","created_by_id":null,"last_modified_by_id":null,"position":3},{"id":3991,"text":"Incubate at room temperature for at least 5 min.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.688Z","updated_at":"2018-12-21T13:35:09.688Z","created_by_id":null,"last_modified_by_id":null,"position":4},{"id":3992,"text":"Absorbance will increase over time; samples should incubate at RT for no more than 1 h.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.703Z","updated_at":"2018-12-21T13:35:09.703Z","created_by_id":null,"last_modified_by_id":null,"position":5},{"id":3993,"text":"Measure absorbance at 595 nm.","checked":false,"checklist_id":969,"created_at":"2018-12-21T13:35:09.710Z","updated_at":"2018-12-21T13:35:09.710Z","created_by_id":null,"last_modified_by_id":null,"position":6}]}],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]}]}],"results":[]},{"my_module":{"id":2094,"name":"Centrifugation","due_date":null,"description":null,"x":209,"y":91,"my_module_group_id":null,"created_at":"2018-11-08T10:28:48.399Z","updated_at":"2018-12-18T14:21:05.140Z","archived":true,"archived_on":"2018-12-18T14:21:05.000Z","created_by_id":202,"last_modified_by_id":null,"archived_by_id":202,"restored_by_id":null,"restored_on":null,"nr_of_assigned_samples":0,"workflow_order":-1,"experiment_id":423,"state":"uncompleted","completed_on":null,"electronic_signature_status":"unlocked","electronic_signature_status_locked_at":null},"outputs":[],"my_module_tags":[],"task_comments":[],"my_module_repository_rows":[],"user_my_modules":[],"protocols":[{"protocol":{"id":3401,"name":null,"authors":null,"description":null,"added_by_id":null,"my_module_id":2094,"team_id":1,"protocol_type":"unlinked","parent_id":null,"parent_updated_at":null,"archived_by_id":null,"archived_on":null,"restored_by_id":null,"restored_on":null,"created_at":"2018-11-08T10:28:48.464Z","updated_at":"2018-11-08T10:28:48.668Z","published_on":null,"nr_of_linked_children":0},"protocol_protocol_keywords":[],"steps":[{"step":{"id":4271,"name":"Centrifugation of samples","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp\u003eSwitch on and follow the manufacturer's instructions to set the centrifugation conditions (attached file). \u003cbr\u003e\u003cbr\u003eFor small sample volumes or proteins that adsorb non-specifically to filters, centrifuge at 10 000 x g for 15 minutes.\u003cbr\u003eFor cell lysates, centrifuge at 40 000–50 000 x g for 30 minutes\u003cbr\u003e\u003cbr\u003eClose and lock the lid and then start the centrifuge cycle. 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Pouring down a glass rod held against the wall of the column will minimize the introduction of air bubbles. \u003cstrong\u003eImmediately fill the column with buffer\u003c/strong\u003e. Mount the column top piece and connect to a pump. Open the column outlet and set the pump to the desired flow rate. If the recommended flow rate cannot be obtained, use the maximum flow rate the pump can deliver. \u003cstrong\u003eDo not exceed the maximum operating pressure of the medium or column.\u003c/strong\u003e Maintain the packing flow rate for at least 3 column volumes after a constant bed height is obtained. Mark the bed height on the column. 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Proteins can be monitored at\u003cstrong\u003e 280 nm.\u003c/strong\u003e\u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":2,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-11-08T10:28:49.408Z","updated_at":"2018-12-21T13:31:50.804Z","last_modified_by_id":202,"protocol_id":3407},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":4290,"name":"Polishing","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\u003cp\u003e\u003cstrong\u003eEquilibrate with 2 column volumes of the buffer\u003c/strong\u003e at a recommended flow rate (See the table). Apply a sample volume equivalent to between 0.3% and 4% of the bed volume. For most applications, the sample volume should not exceed 2% to achieve high resolution. Smaller sample volumes generally lead to an improved resolution. \u003cbr\u003e\u003cstrong\u003eElute with 1 column volume of buffer solution\u003c/strong\u003e (10 to 50 mM sodium phosphate, 150 mM sodium chloride, pH 7.0 to 7.4, or select the buffer in which the sample should be stored or solubilized for the next step). The sample should be fully dissolved. Centrifuge or filter to remove particulate matter.\u003c/p\u003e\u003c/body\u003e\u003c/html\u003e","position":1,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-11-08T10:28:49.496Z","updated_at":"2018-12-21T13:31:21.770Z","last_modified_by_id":202,"protocol_id":3407},"checklists":[],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[{"id":439,"step_id":4290,"table_id":555}],"tables":[{"id":555,"created_at":"2018-11-08T10:28:49.522Z","updated_at":"2018-12-21T13:31:21.773Z","created_by_id":202,"last_modified_by_id":202,"name":"Separation options","team_id":1,"contents":"eyJkYXRhIjpbWyJGcmFjdGlvbmF0aW9uIHJhbmdlLCBNciAoZ2xvYnVsYXIg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\nIDUwICIsIjIiLCIwLDA3NSJdXX0=\n","data_vector":"JzAnOjM3LDUyLDY3LDgyLDk3LDExMiwxMjcsMTQyICcwNzUnOjUzLDE0MyAn\nMSc6MjQsMzksOTksMTE0LDEyOSAnMTAyJzoyNyw0Miw1Nyw3Miw4NywxMDIs\nMTE3LDEzMiAnMTAzJzozMiw0Nyw2Miw3Nyw5MiwxMDcsMTIyLDEzNyAnMic6\nNTEsOTYsMTQxICcyMjcnOjI2LDMxLDQxLDQ2LDU2LDYxLDcxLDc2LDg2LDkx\nLDEwMSwxMDYsMTE2LDEyMSwxMzEsMTM2ICcyNSc6MzMsNjMsMTA4ICcyNjVs\nJzoxMCAnMyc6MzYsNTQsNjYsNjksODEsODQsMTExLDEyNiAnMzAyJzo5ICcz\nMDMnOjI1LDMwLDQwLDQ1LDU1LDYwLDcwLDc1LDg1LDkwLDEwMCwxMDUsMTE1\nLDEyMCwxMzAsMTM1ICc0Jzo0OCw3OCw5MywxMjMsMTM4ICc0NSc6ODMsMTI4\nICc1MCc6NTAsODAsOTUsMTI1LDE0MCAnNTAwJzozNSw2NSwxMTAgJzYnOjEw\nNCwxMTksMTM0ICc3JzoyOSw0NCw1OSw3NCw4OSAnNzUnOjk4LDExMyAnOCc6\nMzgsNjggJ2JlZCc6MTcgJ2NhcGFjaXR5Jzo4ICdkcm9wJzoxMyAnZmxvdyc6\nMjEgJ2ZyYWN0aW9uYXRpb24nOjEgJ2dsb2J1bGFyJzo0ICdtbC9taW4nOjIz\nICdtcGEnOjE4ICdtcic6MyAnb3BlcmF0aW5nJzoyMCAnb3Zlcic6MTQgJ3Bh\nY2tlZCc6MTYgJ3ByZXNzdXJlJzoxMiAncHJvdGVpbnMnOjUgJ3JhbmdlJzoy\nICdyYXRlJzoyMiAncmVjb21tZW5kZWQnOjE5ICdzYW1wbGUnOjYgJ3RoZSc6\nMTUgJ3RvJzoyOCwzNCw0Myw0OSw1OCw2NCw3Myw3OSw4OCw5NCwxMDMsMTA5\nLDExOCwxMjQsMTMzLDEzOSAndHlwaWNhbCc6MTEgJ3ZvbHVtZSc6Nw==\n"}]},{"step":{"id":5224,"name":"For the first time use","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\n\u003cdiv style=\"text-align: justify;\"\u003eRemove storage solution. Applying 2 column volume of distilled water at room temperature. Use a low flow rate to avoid gap formation. Perform a column performance test (see below) and \u003cstrong\u003edetermine the limit for maximum pressure over the packed bed is recommended.\u003c/strong\u003e If this has already been done, go to Step 2.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eColumn efficiency test (the efficiency and peak asymmetry can be determined as follows): \u003c/strong\u003e\u003cbr\u003e\u003cbr\u003e\n\u003c/div\u003e\n\u003col\u003e\n\u003cli style=\"text-align: justify;\"\u003e\n\u003cdiv\u003eEquilibrate the packed column in distilled water or buffer at the flow rate recommended in the product instructions. \u003c/div\u003e\n\u003c/li\u003e\n\u003cli style=\"text-align: justify;\"\u003e\n\u003cdiv\u003eInject 2% acetone (20mg/mL in water) in a volume equivalent to 0.2% to 0.4% of the geometrical bed volume. \u003c/div\u003e\n\u003c/li\u003e\n\u003cli style=\"text-align: justify;\"\u003e\n\u003cdiv\u003eMonitor UV absorbance at 280 nm and determine the elution volume for acetone. \u003c/div\u003e\n\u003c/li\u003e\n\u003cli style=\"text-align: justify;\"\u003e\n\u003cdiv\u003e\n\u003cstrong\u003eCalculate column efficiency\u003c/strong\u003e, that is, the number of theoretical plates per meter (N/m). 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If the protein sample has been highly purified and contains only one protein, the results would show a single protein band after SDS-PAGE separation. However, when there are multiple proteins in the protein samples, different proteins can be separated into multiple protein bands through SDS-PAGE. Therefore, SDS-PAGE technology provides a direct way to analyze the purity of protein samples.\u003c/body\u003e\u003c/html\u003e","position":1,"completed":false,"completed_on":null,"user_id":202,"created_at":"2018-12-19T08:41:05.893Z","updated_at":"2018-12-24T09:22:25.629Z","last_modified_by_id":202,"protocol_id":3409},"checklists":[{"checklist":{"id":970,"name":"Guideline:","step_id":5226,"created_at":"2018-12-21T13:36:26.307Z","updated_at":"2018-12-21T13:36:26.307Z","created_by_id":null,"last_modified_by_id":null},"checklist_items":[{"id":3994,"text":"Add 2 µL of 6X SDS loading buffer to 5–10 µL of supernatant from crude extracts, cell lysates or purified fractions as appropriate.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.308Z","updated_at":"2018-12-21T13:36:26.308Z","created_by_id":null,"last_modified_by_id":null,"position":0},{"id":3995,"text":"Vortex briefly and heat for 5 minutes at +90 to +100 °C.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.316Z","updated_at":"2018-12-21T13:36:26.316Z","created_by_id":null,"last_modified_by_id":null,"position":1},{"id":3996,"text":"Load the samples onto an SDS-polyacrylamide gel.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.323Z","updated_at":"2018-12-21T13:36:26.323Z","created_by_id":null,"last_modified_by_id":null,"position":2},{"id":3997,"text":"Run the gel and stain with Coomassie Blue or silver.","checked":false,"checklist_id":970,"created_at":"2018-12-21T13:36:26.329Z","updated_at":"2018-12-21T13:36:26.329Z","created_by_id":null,"last_modified_by_id":null,"position":3}]}],"step_comments":[],"step_assets":[],"assets":[],"step_tables":[],"tables":[]},{"step":{"id":5233,"name":"Protein Identity Analysis: Mass Spectromety","description":"\u003c!DOCTYPE html PUBLIC \"-//W3C//DTD HTML 4.0 Transitional//EN\" \"http://www.w3.org/TR/REC-html40/loose.dtd\"\u003e\n\u003chtml\u003e\u003cbody\u003e\n\u003cdiv\u003eSelect the appropriate MS Instrument. Samples are measured according to Mass Spectrometer manual. After the MS data is collected, the next step is to\u003cstrong\u003e perform a database search to identify the proteins and/or peptides analyzed by MS\u003c/strong\u003e. A number of parameters can affect the outcome of a database search, and, ultimately, search parameters should consider the history of the sample, \u003cstrong\u003esuch as organism, enzymatic or chemical digestion, and reduction/alkylation steps\u003c/strong\u003e. Differences among search engines can include the scoring algorithm, whether it considers data quality, and whether it considers all fragment ion types or only a subset. 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For the standard curve, add 30 µL of water instead of the standard solution. For the unknown protein samples, add 30 µL protein preparation buffer instead. 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