Protein crystallization by design: chymotrypsinogen without precipitants 1 1Edited by I. A. Wilson

Pjura, Philip; Lenhoff, Abraham M.; Leonard, Shonda A.; Gittis, Apostolos G.

doi:10.1006/jmbi.2000.3851

Cited by 56 publications

(54 citation statements)

References 21 publications

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“…Among these studies there are many attempts to understand better the physical aspects of crystal nucleation and growth as well as to improve crystal quality [Carter, 1997;Rayment, 1997Rayment, , 2002Garcia-Ruiz and Moreno, 1997;Huang et al, 1999;Li et al, 1999;Bunick et al, 2000;Pjura et al, 2000;Nollert et al, 2002;Sauter et al, 2002]; crystallization was also studied in magnetic [Ataka and Wakayama, 2002], electric or ultrasonic fields [Taleb et al, 1999;Nanev and Penkova, 2001], under high pressure [Suzuki et al, 2002] and high temperature [Han and Lin, 2000] centrifugation [Pitts, 1992;Lenhoff et al, 1997], levitation [Chung and Trinh, 1998], microgravity [McPherson, 1997;Borgstahl et al, 2001].…”

mentioning

confidence: 99%

Atomic structure of a CK2α human kinase by microfocus diffraction of extra‐small microcrystals grown with nanobiofilm template

Pechkova

Nicolini

2004

J of Cellular Biochemistry

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Extra-small microcrystals of a human kinase CK2alpha were obtained for the first time by the optimization of a recent protein crystallization method based on highly packed protein nanofilm template. Protein crystal induction and growth appear indeed optimal at high surface pressure of the film template yielding high protein orientation and packing. The resulting extra-small CK2alpha microcrystals (of about 20 microm in diameter) was subsequently used for synchrotron radiation diffraction data collection, which proves possible by means of the Microfocus Beamline at the ESRF Synchrotron in Grenoble. The quality of the resulting crystal diffraction patterns and of its resulting atomic structure at 2.4 A resolution proves the unique validity of the above two combined frontier technologies in defining a new approach to structural proteomics capable to solve the atomic structure of proteins so far never been crystallized and of pharmaceutical relevance. Physical explanation in terms of template dipole moments and possibility of generalization of this method to the wide class of proteins not yet crystallized are finally discussed. The structure of our CK2alpha mutant is in the Protein Data Bank (PDB ID Code 1NA7, deposited on 27 November 2002).

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mentioning

confidence: 99%

Atomic structure of a CK2α human kinase by microfocus diffraction of extra‐small microcrystals grown with nanobiofilm template

Pechkova

Nicolini

2004

J of Cellular Biochemistry

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“…These studies showed the B values measured with SIC to closely compare with those using SLS, thereby establishing the use of SIC as an alternative method to measure second virial coefficients of proteins under different solution conditions García, Hadley et al, 2003;Dumetz et al, 2007;Patro & Przybycien, 1996;Pjura et al, 2000;Valente et al, 2005Valente et al, , 2006DeLucas, 2009).…”

Section: Reviewmentioning

confidence: 81%

“…B-value experiments performed on approximately 70 different aqueous and membrane proteins clearly demonstrate the potential of the values as a diagnostic for initial crystallization conditions as well as for improving existing crystallization conditions (Berger et al, 2005(Berger et al, , 2006Dumetz et al, 2007;García, Hadley et al, 2003;Patro & Przybycien, 1996;Pjura et al, 2000;Tessier & Lenhoff, 2003;Tessier, Vandrey et al, 2002;Valente et al, 2005). However, in spite of the demonstrated capability of SLS B-value measurements to serve as a diagnostic for solution conditions that are more likely to result in crystals, this experimental approach has not gained traction within the crystallographic community.…”

Section: Reviewmentioning

confidence: 99%

Applications of the second virial coefficient: protein crystallization and solubility

Wilson

DeLucas

2014

Acta Crystallogr F Struct Biol Commun

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This article begins by highlighting some of the ground-based studies emanating from NASA's Microgravity Protein Crystal Growth (PCG) program. This is followed by a more detailed discussion of the history of and the progress made in one of the NASA-funded PCG investigations involving the use of measured second virial coefficients (Bvalues) as a diagnostic indicator of solution conditions conducive to protein crystallization. A second application of measuredBvalues involves the determination of solution conditions that improve or maximize the solubility of aqueous and membrane proteins. These two important applications have led to several technological improvements that simplify the experimental expertise required, enable the measurement of membrane proteins and improve the diagnostic capability and measurement throughput.

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“…(3.9), whereas two-body interactions (B mm ) can easily be measured experimentally by traditional light scattering technique [48]. Several other analytical techniques, including membrane osmometry [51][52][53], sedimentation equilibrium [54], selfinteraction chromatography (SIC) [55][56][57] and SEC [24], have been used over the past decade for the measurement of SVC. Except light scattering [48,49,58], no other technique was ever investigated to show how close the experimentally obtained SVC is to the McMillan-Mayers's B mm .…”

Section: Activity Coefficient and Virial Coefficients Of Aqueous Solumentioning

confidence: 99%

A generalized approach to thermodynamic properties of biomolecules for use in bioseparation process design

Ahamed

Ottens

Nfor

et al. 2006

Fluid Phase Equilibria

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Protein crystallization by design: chymotrypsinogen without precipitants 1 1Edited by I. A. Wilson

Cited by 56 publications

References 21 publications

Atomic structure of a CK2α human kinase by microfocus diffraction of extra‐small microcrystals grown with nanobiofilm template

Atomic structure of a CK2α human kinase by microfocus diffraction of extra‐small microcrystals grown with nanobiofilm template

Applications of the second virial coefficient: protein crystallization and solubility

A generalized approach to thermodynamic properties of biomolecules for use in bioseparation process design

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