TY - JOUR
T1 - Crystallization technique of high-quality protein crystals controlling surface free energy
AU - Koizumi, Haruhiko
AU - Uda, Satoshi
AU - Tsukamoto, Katsuo
AU - Tachibana, Masaru
AU - Kojima, Kenichi
AU - Okada, Junpei
AU - Nozawa, Jun
N1 - Funding Information:
*E-mail: h_koizumi@imr.tohoku.ac.jp. ORCID Haruhiko Koizumi: 0000-0001-8355-0320 Jun Nozawa: 0000-0001-7735-3515 Funding This work was supported in part by a Grant-in-Aid for Scientific Research (C) (No. 16K06708) from the Ministry of Education, Culture, Sports, Science and Technology of Japan. Notes The authors declare no competing financial interest.
Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/12/6
Y1 - 2017/12/6
N2 - The relationship between protein crystal quality and growth kinetics was assessed by measuring the normal growth rates vs supersaturation of the (110) and (101) faces of dislocation-free tetragonal hen egg white lysozyme crystals at three precipitant concentrations, with NaCl as the precipitant. Assuming a two-dimensional birth and spreading nucleation mechanism, an increase in the surface free energy of the step edges was realized with increasing NaCl concentration, as established by decreases in the full width at halfmaximum values of X-ray diffraction rocking curves obtained from crystals. These results demonstrate that controlling the surface free energy of the step edges is an important aspect of obtaining high-quality protein crystals. This work also proposes a mechanism for the observed improvements in the crystal quality, based on the reduced incorporation of impurities into the steps during crystal growth.
AB - The relationship between protein crystal quality and growth kinetics was assessed by measuring the normal growth rates vs supersaturation of the (110) and (101) faces of dislocation-free tetragonal hen egg white lysozyme crystals at three precipitant concentrations, with NaCl as the precipitant. Assuming a two-dimensional birth and spreading nucleation mechanism, an increase in the surface free energy of the step edges was realized with increasing NaCl concentration, as established by decreases in the full width at halfmaximum values of X-ray diffraction rocking curves obtained from crystals. These results demonstrate that controlling the surface free energy of the step edges is an important aspect of obtaining high-quality protein crystals. This work also proposes a mechanism for the observed improvements in the crystal quality, based on the reduced incorporation of impurities into the steps during crystal growth.
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U2 - 10.1021/acs.cgd.7b01315
DO - 10.1021/acs.cgd.7b01315
M3 - Article
AN - SCOPUS:85047549937
VL - 17
SP - 6712
EP - 6718
JO - Crystal Growth and Design
JF - Crystal Growth and Design
SN - 1528-7483
IS - 12
ER -