FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1551566995> ?p ?o ?g. }

• W1551566995 abstract "The purposes of our research were: (1) To develop an economical, easy to use, automated, high throughput system for large scale protein crystallization screening. (2) To develop a new protein crystallization method with high screening efficiency, low protein consumption and complete compatibility with high throughput screening system. (3) To determine the structure of lactate dehydrogenase complexed with NADH by x-ray protein crystallography to study its inherent structural properties. Firstly, we demonstrated large scale protein crystallization screening can be performed in a high throughput manner with low cost, easy operation. The overall system integrates liquid dispensing, crystallization and detection and serves as a whole solution to protein crystallization screening. The system can dispense protein and multiple different precipitants in nanoliter scale and in parallel. A new detection scheme, native fluorescence, has been developed in this system to form a two-detector system with a visible light detector for detecting protein crystallization screening results. This detection scheme has capability of eliminating common false positives by distinguishing protein crystals from inorganic crystals in a high throughput and non-destructive manner. The entire system from liquid dispensing, crystallization to crystal detection is essentially parallel, high throughput and compatible with automation. The system was successfully demonstrated by lysozyme crystallization screening. Secondly, we developed a new crystallization method with high screening efficiency, low protein consumption and compatibility with automation and high throughput. In this crystallization method, a gas permeable membrane is employed to achieve the gentle evaporation required by protein crystallization. Protein consumption is significantly reduced to nanoliter scale for each condition and thus permits exploring more conditions in a phase diagram for given amount of protein. In addition, evaporation rate can be controlled or adjusted in this method during the crystallization process to favor either nucleation or growing processes for optimizing crystallization process. The protein crystals gotten by this method were experimentally proven to possess high x-ray diffraction qualities. Finally, we crystallized human lactate dehydrogenase 1 (H4) complexed with NADH and determined its structure by x-ray crystallography. The structure of LDH/NADH displays a significantly different structural feature, compared with LDH/NADH/inhibitor ternary complex structure, that subunits in LDH/NADH complex show open conformation or two conformations on the active site while the subunits in LDH/NADH/inhibitor are all in close conformation. Multiple LDH/NADH crystals were obtained and used for x-ray diffraction experiments. Difference in subunit conformation was observed among the structures independently solved from multiple individual LDH/NADH crystals. Structural differences observed among crystals suggest the existence of multiple conformers in solution." @default.
• W1551566995 created "2016-06-24" @default.
• W1551566995 creator A5090942170 @default.
• W1551566995 date "2006-08-09" @default.
• W1551566995 modified "2023-10-16" @default.
• W1551566995 title "Automated High Throughput Protein Crystallization Screening at Nanoliter Scale and Protein Structural Study on Lactate Dehydrogenase" @default.
• W1551566995 cites W409776901 @default.
• W1551566995 doi "https://doi.org/10.2172/892735" @default.
• W1551566995 hasPublicationYear "2006" @default.
• W1551566995 type Work @default.
• W1551566995 sameAs 1551566995 @default.
• W1551566995 citedByCount "0" @default.
• W1551566995 crossrefType "report" @default.
• W1551566995 hasAuthorship W1551566995A5090942170 @default.
• W1551566995 hasBestOaLocation W15515669951 @default.
• W1551566995 hasConcept C115901376 @default.
• W1551566995 hasConcept C127413603 @default.
• W1551566995 hasConcept C153064111 @default.
• W1551566995 hasConcept C157764524 @default.
• W1551566995 hasConcept C178790620 @default.
• W1551566995 hasConcept C185592680 @default.
• W1551566995 hasConcept C203036418 @default.
• W1551566995 hasConcept C41008148 @default.
• W1551566995 hasConcept C51323132 @default.
• W1551566995 hasConcept C55493867 @default.
• W1551566995 hasConcept C555944384 @default.
• W1551566995 hasConcept C76155785 @default.
• W1551566995 hasConcept C78519656 @default.
• W1551566995 hasConcept C94915269 @default.
• W1551566995 hasConceptScore W1551566995C115901376 @default.
• W1551566995 hasConceptScore W1551566995C127413603 @default.
• W1551566995 hasConceptScore W1551566995C153064111 @default.
• W1551566995 hasConceptScore W1551566995C157764524 @default.
• W1551566995 hasConceptScore W1551566995C178790620 @default.
• W1551566995 hasConceptScore W1551566995C185592680 @default.
• W1551566995 hasConceptScore W1551566995C203036418 @default.
• W1551566995 hasConceptScore W1551566995C41008148 @default.
• W1551566995 hasConceptScore W1551566995C51323132 @default.
• W1551566995 hasConceptScore W1551566995C55493867 @default.
• W1551566995 hasConceptScore W1551566995C555944384 @default.
• W1551566995 hasConceptScore W1551566995C76155785 @default.
• W1551566995 hasConceptScore W1551566995C78519656 @default.
• W1551566995 hasConceptScore W1551566995C94915269 @default.
• W1551566995 hasLocation W15515669951 @default.
• W1551566995 hasLocation W15515669952 @default.
• W1551566995 hasLocation W15515669953 @default.
• W1551566995 hasOpenAccess W1551566995 @default.
• W1551566995 hasPrimaryLocation W15515669951 @default.
• W1551566995 hasRelatedWork W1551566995 @default.
• W1551566995 hasRelatedWork W1978398219 @default.
• W1551566995 hasRelatedWork W2009141905 @default.
• W1551566995 hasRelatedWork W2017400370 @default.
• W1551566995 hasRelatedWork W2053780691 @default.
• W1551566995 hasRelatedWork W2155414586 @default.
• W1551566995 hasRelatedWork W2416800626 @default.
• W1551566995 hasRelatedWork W2748952813 @default.
• W1551566995 hasRelatedWork W2784101170 @default.
• W1551566995 hasRelatedWork W2899084033 @default.
• W1551566995 isParatext "false" @default.
• W1551566995 isRetracted "false" @default.
• W1551566995 magId "1551566995" @default.
• W1551566995 workType "report" @default.