TY - JOUR
T1 - Importance of Determination of Crystal Quality in Protein Crystals when Performing High-Resolution Structural Analysis
AU - Koizumi, Haruhiko
AU - Suzuki, Ryo
AU - Tachibana, Masaru
AU - Tsukamoto, Katsuo
AU - Yoshizaki, Izumi
AU - Fukuyama, Seijiro
AU - Suzuki, Yoshihisa
AU - Uda, Satoshi
AU - Kojima, Kenichi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research (C) (No. 25420694) from the Ministry of Education, Culture, Sports, Science and Technology of Japan. We thank Dr. H. Sugiyama and Dr. K. Hirano of KEK for their help on synchrotron radiation X-ray topography. Monochromatic-beam X-ray topography and XRD rocking-curve measurements were performed at the Photon Factory under the auspices of the Photon Factory Program Advisory Committee of KEK (Proposal Nos. 2014G601, 2015G142).
Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/9/7
Y1 - 2016/9/7
N2 - We show that the extinction effect explained by the dynamical theory of diffraction must be considered even in the case of protein crystals. Equal-thickness fringes, which are attributed to the Pendellösung effect, were clearly observed in the region of a tapered glucose isomerase crystal with wedge-like edges using X-ray topography carried out with a beam of monochromatic synchrotron radiation. This indicates that the perfection of this glucose isomerase crystal is high enough to produce this dynamical theory-related effect: this surely leads to difficulty in the collection of accurate integrated intensities of diffraction spots for X-ray structural analysis. Therefore, it is important to determine whether the crystal quality of a protein crystal under analysis is adequate to obtain accurate three-dimensional structures of protein molecules for X-ray structural analyses. We show that X-ray diffraction rocking-curve measurements can provide clues for this determination.
AB - We show that the extinction effect explained by the dynamical theory of diffraction must be considered even in the case of protein crystals. Equal-thickness fringes, which are attributed to the Pendellösung effect, were clearly observed in the region of a tapered glucose isomerase crystal with wedge-like edges using X-ray topography carried out with a beam of monochromatic synchrotron radiation. This indicates that the perfection of this glucose isomerase crystal is high enough to produce this dynamical theory-related effect: this surely leads to difficulty in the collection of accurate integrated intensities of diffraction spots for X-ray structural analysis. Therefore, it is important to determine whether the crystal quality of a protein crystal under analysis is adequate to obtain accurate three-dimensional structures of protein molecules for X-ray structural analyses. We show that X-ray diffraction rocking-curve measurements can provide clues for this determination.
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U2 - 10.1021/acs.cgd.6b00457
DO - 10.1021/acs.cgd.6b00457
M3 - Article
AN - SCOPUS:84986294146
VL - 16
SP - 4905
EP - 4909
JO - Crystal Growth and Design
JF - Crystal Growth and Design
SN - 1528-7483
IS - 9
ER -