Any feedback?
Literature summary for 3.5.2.6 extracted from
- Improvement of crystal quality by surface mutations of beta-lactamase Toho-1 (2009), Acta Crystallogr. Sect. F, 65, 379-382.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal quality of Toho-1 is improved by using surface modification to remove a sulfate ion involved in crystal packing | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R274N/R276N | sitting-drop vapour-diffusion technique, surface-modified Toho-1 variant does not form merohedrally twinned crystals. Crystals diffract to a significantly higher resolution (0.97 A) than the wild-type crystals (1.65 A) | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | Q47066 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Toho-1 | - |
Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
