Journal: PLoS ONE

Article Title: Selecting Temperature for Protein Crystallization Screens Using the Temperature Dependence of the Second Virial Coefficient

doi: 10.1371/journal.pone.0017950

Figure Lengend Snippet: A): without crystallization agents; B): with crystallization agents. Refer to for detailed solution conditions. Lys.: lysozyme; Pro.K: proteinase K; Con.A: concanavalin A; Chy.A: α -chymotrypsinogen A(II).

Article Snippet: The crystallization trials were set up using an automated protein crystallization robot (Screenmaker 96+8, Innovadyne Technologies Inc. USA).

Techniques: Crystallization Assay

Journal: PLoS ONE

Article Title: Selecting Temperature for Protein Crystallization Screens Using the Temperature Dependence of the Second Virial Coefficient

doi: 10.1371/journal.pone.0017950

Figure Lengend Snippet: The proteins used were as follows: A): lysozyme; B): proteinase K; C): α-chymotrypsinogen A(II); D): concanavalin A. The screening kit was Index™ from Hampton Research. The results showed that a protein yielded higher crystallization success rate at the temperature where the B 22 value of the solution was relatively lower. Error bar: standard error mean; n = 6.

Article Snippet: The crystallization trials were set up using an automated protein crystallization robot (Screenmaker 96+8, Innovadyne Technologies Inc. USA).

Techniques: Crystallization Assay

Journal: PLoS ONE

Article Title: Selecting Temperature for Protein Crystallization Screens Using the Temperature Dependence of the Second Virial Coefficient

doi: 10.1371/journal.pone.0017950

Figure Lengend Snippet: The screening kit was Index™ from Hampton Research. A 1 , A 2 , A 3 : lysozyme crystals obtained at C7; B 1 , B 2 , B 3 : proteinase K crystals obtained at B10; C 1 , C 2 , C 3 : concanavalin A crystals obtained at H8; D 1 , D 2 , D 3 : α -chymotrypsinogen A(II) crystals obtained at G6. Initial concentration of all proteins was 20 mg/mL. A 1 , B 1 , C 1 , D 1 : 277K; A 2 , B 2 , C 2 , D 2 : 289K; A 3 , B 3 , C 3 , D 3 : 301K. This figure shows that the crystal number varied with crystallization temperature as predicted by the measurement of B 22 .

Article Snippet: The crystallization trials were set up using an automated protein crystallization robot (Screenmaker 96+8, Innovadyne Technologies Inc. USA).

Techniques: Concentration Assay, Crystallization Assay

Journal: PLoS ONE

Article Title: Selecting Temperature for Protein Crystallization Screens Using the Temperature Dependence of the Second Virial Coefficient

doi: 10.1371/journal.pone.0017950

Figure Lengend Snippet: Part of the data ( , B and D) in this figure were extracted from published results (n = 7). Crystallization methods: hanging drop. Initial crystallization conditions: A): lysozyme (Lys.) solution: 20 mg/mL in 0.1 M sodium acetate (pH = 4.6), reservoir solution: 60 mg/mL NaCl; B): proteinase K (Pro.K) solution: 20 mg/mL in 25 mM HEPES-Na (pH = 7.0); reservoir solution: 50 mM sodium cacodylate trihydrate, 80 mM Mg(Ac) 2 and 25% w/v PEG 8000 at pH = 6.5; C): α -chymotrypsinogen A(II) (Chy.A) solution: 20 mg/mL α -chymotrypsinogen A(II) in 0.1 M citric acid (pH = 3.5) and 12.5% w/v PEG 3350; reservoir solution: 25% w/v PEG 3350; D): concanavalin A (Con.A) solution: 20 mg/mL in 25 mM HEPES-Na (pH = 7.0); reservoir solution: 0.1 M Tris-HCl and 8% w/v PEG 8000 at pH = 8.5.

Article Snippet: The crystallization trials were set up using an automated protein crystallization robot (Screenmaker 96+8, Innovadyne Technologies Inc. USA).

Techniques: Crystallization Assay