Comparison of solubilities and molecular interactions of BPTI molecules giving different polymorphs

Lafont, Sylvaine; Veesler, Stéphane; Astier, Jean-Pierre; Boistelle, R.

doi:10.1016/s0022-0248(96)00834-2

Cited by 64 publications

(78 citation statements)

References 13 publications

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“…After mixing A and B, the salt concentrations were 1.7 and 1.8 M in NaCl and (NH 4 ) 2 SO 4 solutions, respectively, and the BPTI concentrations were 30 and 10 mg ml À1 in NaCl and (NH 4 ) 2 SO 4 solutions, respectively. These concentrations corresponded to 9 1.6 and 9 1.4, respectively (Lafont et al, , 1997.…”

Section: Proteinsmentioning

confidence: 90%

Protein crystals orientation in a magnetic field

1998

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Nucleation and crystal growth of hen egg-white lysozyme, bovine pancreatic trypsin inhibitor and porcine pancreatic -amylase were carried out in the presence of a magnetic ®eld of 1.25 T produced by small permanent magnets. Crystals were oriented in the magnetic ®eld, except when heterogeneous nucleation occurred. The orientation of protein crystals in the presence of a magnetic ®eld can be attributed to the anisotropic diamagnetic susceptibility of proteins resulting from the large anisotropy of the -helices due to the axial alignment of the peptide bonds.

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Section: Proteinsmentioning

confidence: 90%

Protein crystals orientation in a magnetic field

1998

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“…In another series of experiments, Lafont et al (1997) and Veesler et al (1996) investigated small-angle X-ray scattering experiments near the nucleation point ($30±40 mg ml À1 ). They con®rmed that anions, and particularly thiocyanate, reverse the repulsive effect, leading to the formation of aggregates with a hydrodynamic radius roughly compatible with a tetramer.…”

Section: The Thiocyanate Ions and Their Role In Decamer Buildingmentioning

confidence: 99%

“…less soluble at high temperature). Veesler et al (1996) and Lafont et al (1997) have shown, using small-angle X-ray scattering (SAXS) and quasi-elastic light scattering (QELS) experiments, that during the nucleation process of BPTI using potassium thiocyanate as crystallizing agent the solution is monodispersed, but not monomeric, in the vicinity of the solubility curve. These experiments suggested a unique oligomeric particle to be formed prior to crystallization.…”

Section: Introductionmentioning

confidence: 99%

The decameric structure of bovine pancreatic trypsin inhibitor (BPTI) crystallized from thiocyanate at 2.7 Å resolution

Hamiaux

Prangé

Riès-Kautt

et al. 1999

Acta Crystallogr D Biol Crystallogr

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The structure of a monoclinic form of bovine pancreatic trypsin inhibitor (BPTI) crystallized from a thiocyanate solution has been determined and re®ned at 2.7 A Ê resolution. The space group is P2 1 with a = 71.56, b = 73.83, c = 64.47 A Ê , = 93.9and Z = 20. The ten independent molecules were located by a multi-body molecular-replacement search as developed in the AMoRe program, starting from a single monomer model (PDB code: 6PTI). The molecular arrangement of the subunits is a decamer resulting from the combination of two orthogonal ®vefold and twofold noncrystallographic axes. This builds a globular micelle-like particle which minimizes hydrophobic interactions with the solvent. The re®nement was conducted with non-crystallographic symmetry constraints up to a ®nal residual of R = 0.20 (R free = 0.26). The root-mean-square deviations from ideal geometry were 0.015 A Ê and 1.6 on bond distances and bond angles, respectively. Several sites for thiocyanate ions were analyzed.

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“…These may, in turn, be applied under different physical conditions such as temperature, which can be an important variable in biological macromolecule crystallization, since an understanding of the phase diagram is useful for the production of suitable crystals for structural biology (Boistelle et al 1992;Lafont et al 1994Lafont et al , 1997Revalor et al 2010). …”

Section: Effect Of Temperature On the Solubilitymentioning

confidence: 99%

Crystallization, solubility and thermodynamics of the highly thermostable glucose isomerase from Streptomyces sp. strain

Borgi¹,

Rhimi²,

Kadri³

2014

gpb

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Abstract. The crystallization behaviour of the highly thermostable glucose isomerase from the Streptomyces sp. strain isolated from Tunisian soil was investigated using ammonium sulfate as a precipitating agent. We established phase diagrams at different temperatures and protein concentrations. It was found that the solubility increased with increasing temperature and decreased with increasing salt concentration. The temperature-dependent solubility was used to characterize the thermodynamic parameters of crystallization such as enthalpy, entropy and free energy.

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Comparison of solubilities and molecular interactions of BPTI molecules giving different polymorphs

Cited by 64 publications

References 13 publications

Protein crystals orientation in a magnetic field

Protein crystals orientation in a magnetic field

The decameric structure of bovine pancreatic trypsin inhibitor (BPTI) crystallized from thiocyanate at 2.7 Å resolution

Crystallization, solubility and thermodynamics of the highly thermostable glucose isomerase from Streptomyces sp. strain

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