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Literature summary for 4.2.2.1 extracted from
- Crystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis (2013), Acta Crystallogr. Sect. F, 69, 673-675.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Hyl, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Streptococcus suis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.001 ml of protein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, 1 mM mercaptoethanol, and 1 mM EDTA, is mixed with 0.001 ml of reservoir solution, and equilibrated against 0.25 ml of reservoir solution, a few weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular-replacement method | Streptococcus suis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus suis | - |
gene Hyl | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chomatography, dialysis, gel filtration and ultrafiltration | Streptococcus suis |
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Release 2023.1 (January 2023)
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