Hostname: page-component-7bb8b95d7b-s9k8s Total loading time: 0 Render date: 2024-09-19T16:25:13.787Z Has data issue: false hasContentIssue false
  • English
  • Français

Monitoring protein precipitates by in-house X-ray powder diffraction

Published online by Cambridge University Press:  14 November 2013

Kenny Ståhl ,
Christian G. Frankær ,
Jakob Petersen  and
Pernille Harris
Kenny Ståhl*
Affiliation:
Department of Chemistry, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
Christian G. Frankær
Affiliation:
Department of Chemistry, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
Jakob Petersen
Affiliation:
Department of Chemistry, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
Pernille Harris
Affiliation:
Department of Chemistry, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark
*
a)Author to whom correspondence should be addressed. Electronic mail: kenny@kemi.dtu.dk
Get access Rights & Permissions [Opens in a new window]

Abstract

Powder diffraction from protein powders using in-house diffractometers is an effective tool for identification and monitoring of protein crystal forms and artifacts. As an alternative to conventional powder diffractometers a single crystal diffractometer equipped with an X-ray micro-source can be used to collect powder patterns from 1 µl samples. Using a small-angle X-ray scattering (SAXS) camera it is possible to collect data within minutes. A streamlined program has been developed for the calculation of powder patterns from pdb-coordinates, and includes correction for bulk-solvent. A number of such calculated powder patterns from insulin and lysozyme have been included in the powder diffraction database and successfully used for search-match identification. However, the fit could be much improved if peak asymmetry and multiple bulk-solvent corrections were included. When including a large number of protein data sets in the database some problems can be foreseen due to the large number of overlapping peaks in the low-angle region, and small differences in unit cell parameters between pdb-data and powder data. It is suggested that protein entries are supplied with more searchable keywords as protein name, protein type, molecular weight, source organism etc. in order to limit possible hits.

Keywords

protein powderfingerprintingsearch-matchsolvent correctionlysozymeinsulin
Type
Technical Articles
Information
Powder Diffraction , Volume 28 , Supplement S2 , September 2013 , pp. S458 - S469
Copyright
Copyright © International Centre for Diffraction Data 2013 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Collings, I., Watier, Y., Giffard, M., Dagogo, S., Kahn, R., Bonneté, F., Wright, J. P., Fitch, A. N. and Margiolaki, I. (2010). “Polymorphism of microcrystalline urate oxidase from Aspergillus flavus ,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 539–548 Google Scholar
Oxford Cryosystems (1999). “Crystallographica Search-Match,” J. Appl. Crystallogr. 32, 379–380.Google Scholar
Fokine, A. and Urzhumtsev, A. (2002). “Flat bulk-solvent model: obtaining optimal parameters,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 58, 1387–1392.Google Scholar
Frankær, C. G., Harris, P. and Ståhl, K. (2011). “A sample holder for in-house X-ray powder diffraction studies of protein powders,” J. Appl. Crystallogr. 44, 1288–1290.Google Scholar
Frankær, C. G., Knudsen, M. V., Norén, K., Nazarenko, E., Ståhl, K. and Harris, P. (2012). “The structures of T6, T3R3 and R6 bovine insulin: combining X-ray diffraction and absorption spectroscopy,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 68, 1259–1271.Google Scholar
Frericks Schmidt, H. L., Sperling, L. J., Gao, Y. G., Wylie, B. J., Boettcher, J. M., Wilson, S. R. and Rienstra, C. M. (2007). “Crystal Polymorphism of Protein GB1 Examined by Solid-State NMR Spectroscopy and X-ray Diffraction,” J. Phys. Chem. B. 111, 14362–14369.Google Scholar
Hartmann, C. G., Nielsen, O. F., Ståhl, K., and Harris, P. (2010). “In-house characterization of protein powder,” J. Appl. Crystallogr. 43, 876–882.Google Scholar
Hartmann, C. G., Harris, P., and Ståhl, K. (2011). “In-house characterization of protein powder,” Z. Kristallogr. Proc. 1, 163–168.Google Scholar
Jenner, M. J., Wright, J. P., Margiolaki, I., and Fitch, A. N. (2007). “Successful protein cryocooling for powder diffraction,” J. Appl. Crystallogr. 40, 121–124.Google Scholar
Karavassili, F., Giannopoulou, A. E., Kotsiliti, E., Knight, L., Norrman, M., Schluckebier, G., Drube, L., Fitch, A. N., Wright, J. P. and Margiolaki, I. (2012). “Structural studies of human insulin cocrystallized with phenol or resorcinol via powder diffraction,” Acta Crystallogr., Sect. D: Biol. Crystallogr. 68, 1632–1641.Google Scholar
Margiolaki, I., and Wright, J. P. (2008). “Powder crystallography on macromolecules,” Acta Crystallogr., Sect. A: Found. Crystallogr. 64, 169–180.Google Scholar
Norrman, M., Ståhl, K., Schluckebier, G. and Al-Karadaghi, S. (2006). “Characterization of insulin microcrystals using powder diffraction and multivariate data analysis,” J. Appl. Crystallogr. 39, 391–400.Google Scholar
Phillips, S. E. V. (1980). “Structure and Refinement of Oxymyoglobin at 1.6 Å Resolution,” J. Mol. Biol., 142, 531–554.Google Scholar
Sato, T., Yamada, Y., Saijo, S., Hori, T., Hirose, R., Tanaka, N., Sazaki, G., Nakajima, K., Igarashi, N., Tanaka, M. and Matsuura, Y. (2001). “Improvement in diffraction maxima in orthorhombic HEWL crystal grown under higher magnetic field,” J. Crystal Growth. 232, 229–236.Google Scholar