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Hi Dan,
Yes, you can try the magic chemical for peptides: triflouroethanol
(TFE). I was able to solubilize a mutant of a small 35 amino acid
peptide and crystallized it in the presence of 15% v/v TFE. TFE
increased the solubility from ~20mg/ml to ~100mg/ml. For another mutant,
I got heavy precipitate and multiple nucleation without TFE, but after
adding 15% TFE to the reservoir solutions of the same plate, obtained
crystals which diffracted to 1A resolution. However, do not use too high
a concentration of TFE, as it can affect secondary structure. See JMB
(2006) 359: 546-553 for more info.
good luck,
thang
Kevin Jude wrote:
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One of my coworkers has had success with hydrophobic peptides by
treating them like organic molecules; batch crystallization from
organic phases has worked well. See eg De Simone, Giuseppina;
Lombardi, Angela; Galdiero, Stefania; Nastri, Flavia; Di Costanzo,
Luigi; Gohda, Shin; Sano, Atsuiro; Yamada, Takashi; Pavone, Vincenzo.
The crystal structure of a Dcp-containing peptide. Biopolymers
(2000), 53(2), 182-188.
good luck
kmj
ferrarod wrote:
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Hello everyone,
Sorry for the off topic question. I was wondering if anyone had any
ideas or
suggestions on protein crystallization of a small peptide. It is 46
amino
acids and it is very hydrophobic. It is not soluble in buffered
water, but
it is soluble in 70% acetonitrile and in detergent. We have tried
traditional sparse matrix screens, but we get precipitate even at low
concentrations (i.e. 3 mg/ml). Any advice or suggestions would be
appreciated.
Cheers,
Dan
