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Phoenix protein crystallization robot

Manufactured by Art Robbins Instruments
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The Phoenix protein crystallization robot is a laboratory instrument designed for automated protein crystallization screening. It is capable of preparing and dispensing nanoliter-scale droplets of protein samples and crystallization solutions into multi-well plates, facilitating the systematic exploration of crystallization conditions.

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Lab products found in correlation

24 well plate, by Hampton Research (2 mentions) 96 well plates, by Art Robbins Instruments (2 mentions) Index screen, by Hampton Research (1 mentions) Crystallization kits, by Hampton Research (1 mentions) Cryoloop, by Hampton Research (1 mentions)

4 protocols using phoenix protein crystallization robot

1

Crystallization of pHLA Complexes

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The crystal screening for purified pHLA complexes was initiated using commercial kits (Hampton Research). The pHLA complexes and crystallization solution drops were dispensed in equal volumes (1:1) by employing Phoenix protein crystallization robot (Art Robbins Instruments) in 96 well plates (Art Robbins Instruments) and plates were incubated at 16 °C. After the initial hits were obtained, the crystal drops for pHLA complexes were set using hanging drop vapour diffusion method in 24 well plates (Hampton Research) and plates were incubated at 16 °C. The crystals for HLA-A*11:01-ATIGTAMYK (9-mer) complex were formed in condition containing 0.2 M lithium sulfate, 0.1 M Tris pH 8.5, 30% PEG 4000. For the HLA-A*11:01-ATIGT (5-mer) + AMYK (4-mer) complex, crystals were formed in condition containing 0.2 M sodium malonate pH 5.0, 20% PEG 3350. The pHLA complex crystals were harvested by soaking in a reservoir solution supplemented with 20% glycerol as a cryo-protectant, and stored in liquid nitrogen before use.
Huan X., Zhuo Z., Xiao Z, & Ren E.C. (2019). Crystal structure of suboptimal viral fragments of Epstein Barr Virus Rta peptide-HLA complex that stimulate CD8 T cell response. Scientific Reports, 9, 16660.
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2

Crystallization of Silver-Loaded CusS Protein

Cited 1 time
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The pTXB3-CusS(39-187) plasmid was used for expression of CusS(39-187)11 (link). Apo CusS(39-187) and silver loaded CusS(39-187) (Ag(I)-CusS(39-187)) were prepared as previously described11 (link). Ag(I)-CusS(39-187) in 25 mM MES pH 6.0 buffer was concentrated to 7–8 mg/mL for crystallization. Initial crystallization of Ag(I)-CusS(39-187) was performed with commercially-available Index HT screening solutions (Hampton Research). Droplets consisting of 0.2 μL protein solution and 0.2 μL of each precipitant solution were mixed in sitting drops in a 96-well plate using a PHOENIX protein crystallization robot (Art Robbins Instruments). Clusters of rod-shaped crystals of CusS(39-187) formed after one week in a precipitant solution containing 100 mM Tris-HCl pH 8.5, 200 mM ammonium acetate, and 25% PEG-3350 at 4°C. The crystallization conditions were further optimized in the initial precipitant solution with varying PEG-3350 percentages and protein:precipitant ratios using sitting-drop vapor-diffusion at 4°C. Clusters of crystals were observed in all drops containing 100 mM Tris-HCl pH 8.5, 200 mM ammonium acetate, and 25% PEG-3350 with 1:2 protein:precipitant ratio. Diffraction quality protein crystals were obtained by equilibrating droplets against 1 mL precipitant solution using the sitting-drop vapor-diffusion method at 4°C. Crystals were flash frozen in liquid nitrogen.
Affandi T., Issaian A.V, & McEvoy M.M. (2016). The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface. Biochemistry, 55(37), 5296-5306.
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3

Optimized Protein Crystallization Protocol

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Initial crystallization conditions were identified with a sparse matrix screening approach (Index Screen, Hampton Research, Aliso Viejo, USA) and a Phoenix protein crystallization robot (Art Robbins Instruments, Sunnyvale, USA) [60] . The crystallization conditions were optimized in a hanging drop vapor diffusion setup and involved microseeding. Crystals of diffraction quality were obtained by mixing 1 µL of protein solution with 1 µL of reservoir solution and equilibrating the droplet of 2 µL against 700 µL reservoir solution [0.4 M magnesium formate, 15% (w/v) PEG 3350]. The crystals were soaked in cryo-solution [0.4 M magnesium formate, 15% (w/v) PEG 3350, 15% (v/v) ethylenglycol or 20% (v/v) dimethyl sulfoxide (DMSO)] prior to flash-cooling in liquid nitrogen.
Scherer M., Klingl S., Sevvana M., Otto V., Schilling E.M., Stump J.D., Müller R., Reuter N., Sticht H., Muller Y.A, & Stamminger T. (2014). Crystal Structure of Cytomegalovirus IE1 Protein Reveals Targeting of TRIM Family Member PML via Coiled-Coil Interactions. PLoS Pathogens, 10(11), e1004512.
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4

Crystallization of pHLA Complexes

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Commercially available crystallization kits from Hampton Research were used to initiate the crystal screening for purified pHLA complexes. By employing Phoenix protein crystallization robot (Art Robbins Instruments), the pHLA complexes and crystallization solution drops were dispensed in equal volumes (1:1) into 96 well plates (Art Robbins Instruments). After setting crystal screening, plates were incubated at 20 °C. Once the initial hits were obtained, the crystal drops for pHLA complexes were set using hanging drop vapor diffusion method in 24 well plates (Hampton Research) and plates were incubated at 20 °C. The crystals for HLA-B*58:01-KAGQVVTIW in the absence of allopurinol and oxypurinol, and HLA-B*58:01-KAGQVVTI complex in the presence of 10 µg/ml allopurinol formed in condition containing 0.2 M sodium thiocyanate pH 6.9, 20% w/v polyethylene glycol 3350. Protein crystals of HLA-B*58:01-VSFIEFVGW in the absence of allopurinol and oxypurinol, and HLA-B*58:01-VSFIEFVI in the presence of 10 µg/ml allopurinol formed in condition containing 0.04 M citric acid, 0.06 M bis–Tris propane pH 6.4, 20% w/v polyethylene glycol 3350. The pHLA complex crystals were cryo-protected by soaking in a reservoir solution supplemented with 20% glycerol, harvested by different sized CryoLoops (Hampton Research) and stored in liquid nitrogen before use.
Huan X., Zhuo N., Lee H.Y, & Ren E.C. (2023). Allopurinol non-covalently facilitates binding of unconventional peptides to HLA-B*58:01. Scientific Reports, 13, 9373.
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