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At least 1,135 records · Page 63Linked to original sources
PubMed1996

Lamellar stacking in three-dimensional crystals of Ca(2+)-ATPase from sarcoplasmic reticulum.

Electron microscopy of multilamellar crystals of CA(2+)-ATPase currently offers the best opportunity for obtaining a high-resolution structure of this ATP-driven ion pump. Under certain conditions small, wormlike crystals are formed and provide views parallel to the lamellar plane, from which parameters of lamellar stacking can be directly measured. Assuming that molecular packing is the same, data from these views could supplement those obtained by tilting large, thin platelike crystals. However, we were surprised to discover that the lamellar spacing was variable and depended on the amount of glycerol present during crystallization (20% versus 5%). Projection maps (h,0,l) from these womklike crystals suggest different molecular contacts that give rise to the different lamellar spacings. Based on an orthogonal projection map (h,k,0) from collapsed, wormlike crystals and on x-ray powder patterns, we conclude that molecular packing within the lamellar plane is the same as that in thin, platelike crystals and is unaffected by glycerol. Finally, the orientation of molecules in the lamellar plane was characterized from freeze-dried, shadowed crystals. Comparing the profile of molecules in these multilamellar crystals with that previously observed in helical tubes induced by vanadate gives structural evidence of the conformational change that accompanies binding of calcium of Ca(2+)-ATPase.

Animals↗
PubMed2003

Microscopy and calorimetry as complementary techniques to analyze sugar crystallization from amorphous systems.

A comparison of microscopic and macroscopic techniques to evaluate sugar crystallization kinetics is presented using amorphous lactose and lactose-trehalose mixtures. Polarized light video microscopy (PLV) and differential scanning calorimetry (DSC) were applied to measure crystallization kinetics, induction times and time for complete sugar crystallization at different storage temperatures (60-95 degrees C). DSC was also employed to measure the glass transition temperature (T(ag)) of the systems. PLV permitted direct observation, in real time, of growth of individual crystals and morphological aspects at a scale not detected by DSC. Taking the average of several microscopic observations, the results for temperature dependence of crystallization rate and time to complete lactose crystallization were similar to those obtained by DSC. Both PLV and DSC techniques showed that the presence of trehalose delayed lactose crystallization, without affecting the T(ag) value. For the analysis of sugar crystallization in amorphous systems, PLV and DSC proved to be complementary techniques. Validation of results obtained by PLV with results from DSC opens a new area of microstructural analysis of crystallizing systems.

Calorimetry, Differential Scanning↗
PubMed2000

Role of anionic proteins in kidney stone formation: interaction between model anionic polypeptides and calcium oxalate crystals.

PURPOSE: We tested the effect of molecular weight and amino acid composition (aspartate versus glutamate) in model peptides on calcium oxalate dihydrate (COD) formation to understand how known urinary inhibitor proteins might control spontaneous crystallization. MATERIALS AND METHODS: Supersaturated solutions of CaCl2 and Na2C2O4 in HEPES buffered saline solution were prepared at various calcium (Ca) to oxalate (Ox) ratios, but constant supersaturation, in the presence of protein inhibitors (polyaspartic acid molecular weight series or polyglutamic acid). The resulting crystals were collected and evaluated with optical microscopy. RESULTS: With no added inhibitors, the crystal size increased with Ca to Ox ratio, while the number of crystals decreased. With protein inhibitors at equivalent mass concentrations, intermediate molecular weight proteins produced a greater proportion of COD in Ca rich conditions than did either extreme. In Ox rich conditions, the proportion of COD was directly related to protein molecular weight. However, at equivalent molar concentrations, the proportion of COD produced was directly related to molecular weight under all conditions. Larger protein concentrations were required to produce COD at high Ox conditions, in proportion to the increased number of crystals produced. Polyglutamic acid had a much weaker effect on crystal structure, but it changed the COM morphology. CONCLUSIONS: The results suggest that a discrete number of protein molecules per crystal were required to direct crystallization toward COD, and that a characteristic size of polypeptide chain can be defined. The charge of the side group was not the sole determinant of this effect, as polyglutamic and polyaspartic acids behaved differently. Calcium oxalate crystal nucleation rates appeared to increase with Ox content.

Calcium Oxalate↗
PubMed1989

A study of the incorporation of urinary macromolecules onto crystals of different mineral compositions.

A new method used to study the binding of proteins onto calcium oxalate crystals demonstrated this interaction to be a selective process regarding the types of adsorbed proteins. To determine whether the incorporation of urinary macromolecules onto crystals formed in urine in vitro is dependent on the specific crystalline composition, this technique was applied to both uric acid and calcium oxalate crystals. Powdered uric acid was dissolved in urine and the pH lowered to 5.5. The resulting uric acid crystals were centrifuged and the pellet dialyzed against water at pH 8.0. Calcium oxalate crystals produced by the addition of 0.1 M calcium chloride and 0.1 M sodium oxalate to an aliquot of the same urine sample were demineralized with 5% EDTA. Gel filtration chromatography was used to isolate the protein fraction of an aliquot of the urine samples before and after crystallization of uric acid and calcium oxalate. The proteins recovered from the crystals and urine samples were separated by two-dimensional polyacrylamide gel electrophoresis. Analysis of the gels confirmed that the binding of urinary proteins onto crystals is a selective process and indicate that this interaction is dependent on the specific inorganic composition of the crystals.

Adult↗
PubMed1985

Inhibition of sodium urate crystal adherence to bladder surface by polysaccharide.

Bladder surface glycosaminoglycan (polysaccharide) has been shown to act in a nonspecific manner as an antiadherence factor and may potentially be important in the pathogenesis (and prevention) of renal calculi. It has been shown that when present, bladder surface GAG will reduce the adherence of both calcium and calcium oxalate crystals. This study was conducted to see if a similar effect would be found with uric acid crystals, in that the presence of the normal bladder mucus with its contained GAG and exogenously supplied polysaccharide, pentosanpolysulfate, would be inhibitory to crystal adherence. Radioactively labeled uric acid crystals were made by dissolving 14C labeled sodium urate to a point of saturation at pH 7.5 and then rapidly lowering the pH to 5.5. These crystals were placed into four groups of bladders: 1) normal bladders, 2) bladders rendered mucus deficient with hydrochloric acid, 3) mucus deficient bladders which were pre-treated with sodium pentosanpolysulfate prior to crystal addition and 4) mucus deficient bladders to which were added crystals pretreated with pentosanpolysulfate. There was a significant rise in crystal adherence after acid treatment of the bladder, a 2.3-fold increase, which was blocked with prior treatment of the crystals with pentosanpolysulfate and to a lesser degree by pretreating mucus deficient bladders with pentosanpolysulfate.

Animals↗
PubMed1980

Calcium oxalate crystalluria: crystal size in urine.

Studies of calcium oxalate crystals in urine suggest similarities to crystal growth in calcium oxalate renal calculi. Previous reports indicate that urinary crystals in patients in whom stones form are larger than those in normal subjects. We report herein a study on crystal size by structure and habit (shape) based on direct microscopic measurement of crystals in urine of 27 normal subjects and in 6 of 22 patients in whom stones form. The mean size of all crystals in normal subjects is 12.0 plus or minus 7.8 micrometers. Calcium oxalate monohydrate crystals are significantly smaller than calcium oxalate dihydrate (p less than 0.01). In 22 patients with stones there was no correlation between crystalluria and severity or duration of disease. The mean crystal size in 6 patients did not support the conclusion that patients in whom stones form excrete larger crystals than normal subjects.

Calcium Oxalate↗
PubMed2002

Crystallization of membrane proteins in cubo.

Our understanding of lipidic cubic phases for the crystallization of membrane proteins has advanced greatly since the inception of the concept in 1996, and the method is becoming well accepted. Several protocols that allow the efficient screening of crystallization conditions and handling of crystals are presented. State-of-the art micro techniques allow a large number of crystallization conditions to be tested using very small amounts of protein, and diffraction quality crystals can be grown in larger volumes in glass vials. In cubo crystallization conditions differ from those employed for detergent-solubilized proteins. Variations comprise the type of lipid matrix, detergent, protein, salt, temperature, hydration, pH, and pressure. Commercially available screening kits may be applied in order to define lead conditions. Once obtained, crystals may be removed from the surrounding cubic phase mechanically, by enzymatic hydrolysis, or by detergent solubilization. We anticipate this set of protocols to be applied successfully to larger, less stable, and noncolored membrane proteins in order to obtain well-diffracting crystals of membrane proteins that have so far evaded crystallization in the detergent-solubilized state.

Crystallization↗
PubMed1998

Oriented growth of calcium oxalate monohydrate crystals beneath phospholipid monolayers.

Oriented calcium oxalate crystals have been grown beneath phospholipid monolayers at the air-solution interface from supersaturated calcium oxalate solutions. Mature calcium oxalate crystals grown beneath zwitterionic dipalmitoylphosphatidylcholine (DPPC) monolayers exhibit the characteristic morphology of calcium oxalate monohydrate (COM) crystals with the elongated (101) crystal face preferentially oriented parallel to the plane of the monolayer. Calcium oxalate crystals grown beneath negatively-charged dimyristoylphosphatidylserine (DMPS) monolayers also show a preferential orientation with respect to the monolayer; they do not, however, exhibit the characteristic COM morphology. Raman spectroscopy strongly suggests that the crystals grown beneath either DPPC or DMPS monolayers are the monohydrate phase of calcium oxalate; therefore, differences in crystal morphology are not due to differences in the crystalline phase. Dimyristoylphosphatidylethanolamine (DMPE), dimyristoylphosphatidic acid (DMPA), eicosanoic acid (C20), and eicosanol (C20-OH) monolayers have also been studied to help elucidate the mechanisms of interaction between the lipid monolayers and the calcium oxalate crystals. We discuss the roles of lattice matching, hydrogen bonding, stereochemistry and electrostatics on crystal orientation and morphology.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1996

Gammopathy-related crystal-storing histiocytosis, pseudo- and pseudo-pseudo-Gaucher cells. Critical commentary and mini-review.

Commenting on a case report of dermal immunocytoma with crystal-storing histiocytes, a short review is given on the phenomena related to crystallization of monoclonal immunoglobulins within plasma cells, in the extracellular space, or within the lysosomal compartment of macrophages. Paraprotein crystallization is supported by hydrophobicity, poor solubility in the cold or at acid pH, and there are few reports on structural defects of crystal-forming myeloma proteins which are supposed to promote either their crystallization or impaired intralysosomal degradation. In the hitherto known cases of crystal histiocytosis, immunoglobulins of light chain type kappa have been exclusively involved in the process of macrophage storage. Accumulation of paraprotein-related crystals in macrophages may mimic the appearance of Gaucher cells or of the so-called pseudo-Gaucher cells seen in chronic myelogeneous leukaemia. With regard to their lightmicroscopical and ultrastructural differences to both, Gaucher cells and pseudo-Gaucher cells, paraproteinaemia-related crystal-storing macrophages may be denoted as pseudo-pseudo-Gaucher cells (PPGC). Human PPGC are similar to constitutive crystal-storing histiocytes known from inbred C57 BL-6 mice. The distribution of PPGC may be limited to the realm of a plasmacytoma or immunocytoma, but there are also cases with systemic involvement of the RES similar to Gaucher disease.

Animals↗
PubMed2003

Characterization of piroxicam crystal modifications.

Piroxicam polymorphism was extensively studied in the past. The objective of the present work was to evaluate polymorphism of piroxicam once again and to characterize the obtained crystal forms. Three polymorphic forms and one monohydrate form were obtained by crystallization from saturated solutions in various solvents. Polarity of solvents and crystallization rate defined by temperature of crystallization were found to be critical parameters in determining the polymorphic form. A new polymorphic form designated as form III was obtained by forced crystallization using dry ice. Only form I with the highest melting point was found to be stable under mechanical and thermal stress. Differences in IR spectra were attributed mainly to the differences in number and positions of H-bonds in the piroxicam crystal forms. Slow crystallization of piroxicam from absolute ethanol solution resulted in a mixture of form II and monohydrate. Crystal structure analysis proved that form II represents form alpha(2) already proposed in the literature. Differences in dissolution rates among crystal forms of piroxicam were attributed to differences in their wettability, where highest wettability was obtained for monohydrate and the lowest for form III.

Crystallization↗
PubMed1999

Formation and compression characteristics of prismatic polyhedral and thin plate-like crystals of paracetamol.

Prismatic polyhedral crystals of paracetamol were prepared by cooling an aqueous saturated solution of paracetamol from 65 to 25 degrees C. Thin plate-like crystals were prepared by adding a concentrated solution of paracetamol in hot ethanol to water at 3 degrees C. Infrared (IR), X-ray powder diffraction (XPD) and differential scanning calorimetry (DSC) studies confirmed that these two forms of crystals were structurally similar, therefore polymorphic modifications were ruled out. The crystal habit influenced the compression properties during axial compression of paracetamol at different constant rates in a compaction simulator, the Heckel plots and their associated constants being dependent on the habits. The correlation coefficient of the initial part of the Heckel plots, and also the values of strain rate sensitivity (SRS), were lower for thin plate-like crystals, indicative of greater fragmentation for the thin plate-like as compared to polyhedral crystals. Compacts made from thin plate-like crystals exhibited higher elastic recoveries and elastic energies indicating that these crystals underwent less plastic deformation during compression than the polyhedral crystals.

Acetaminophen↗
PubMed2003

Enhancing protein crystallization through precipitant synergy.

Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization.

Animals↗
PubMed2003

Protein crystals and their growth.

Recent results on the associations between protein molecules in crystal lattices, crystal-solution surface energy, elastic properties, strength, and spontaneous crystal cracking are reviewed and discussed. In addition, some basic approaches to understanding the solubility of proteins are followed by an overview of crystal nucleation and growth. It is argued that variability of mixing in batch crystallization may be a source of the variation in the number of crystals ultimately appearing in the sample. The frequency at which new molecules join a crystal lattice is measured by the kinetic coefficient and is related to the observed crystal growth rate. Numerical criteria used to discriminate diffusion- and kinetic-limited growth are discussed on this basis. Finally, the creation of defects is discussed with an emphasis on the role of impurities and convection on macromolecular crystal perfection.

Crystallization↗
PubMed2003

Membrane protein crystallization.

The need for high-resolution structure information on membrane proteins is immediate and growing. Currently, the only reliable way to get it is crystallographically. The rate-limiting step from protein to structure is crystal production. An overview of the current ideas and experimental approaches prevailing in the area of membrane protein crystallization is presented. The long-established surfactant-based method has been reviewed extensively and is not examined in detail here. The focus instead is on the latest methods, all of which exploit the spontaneous self-assembling properties of lipids and detergent as vesicles (vesicle-fusion method), discoidal micelles (bicelle method), and liquid crystals or mesophases (in meso or cubic-phase method). In the belief that a knowledge of the underlying phase science is integral to understanding the molecular basis of these assorted crystallization strategies, the article begins with a brief primer on lipids, mesophases, and phase science, and the related issue of form and function as applied to lipids is addressed. The experimental challenges associated with and the solutions for procuring adequate amounts of homogeneous membrane proteins, or parts thereof, are examined. The cubic-phase method is described from the following perspectives: how it is done in practice, its general applicability and successes to date, and the nature of the mesophases integral to the process. Practical aspects of the method are examined with regard to salt, detergent, and screen solution effects; crystallization at low temperatures; tailoring the cubic phase to suit the target protein; different cubic-phase types; dealing with low-protein samples, colorless proteins, microcrystals, and radiation damage; transport within the cubic phase for drug design, cofactor retention, and phasing; using spectroscopy for quality control; harvesting crystals; and miniaturization and robotization for high-throughput screening. The section ends with a hypothesis for nucleation and growth of membrane protein crystals in meso. Thus far, the bicelle and vesicle-fusion methods have produced crystals of one membrane protein, bacteriorhodopsin. The experimental details of both methods are reviewed and their general applicability in the future is commented on. The three new methods are rationalized by analogy to crystallization in microgravity and with respect to epitaxy. A list of Web resources in the area of membrane protein crystallogenesis is included.

Crystallization↗
PubMed2003

Organization of apatite crystals in human woven bone.

The organization of collagen fibrils differs in woven bone and lamellar bone, and it reflects certain aspects of the nature of the mineral crystals associated with them. In order to investigate the morphology and distribution of apatite crystals in woven bone, mineralized collagen fibrils and isolated crystals from the mid-diaphyses of human fetal femurs were observed with scanning and transmission electron microscopy and high-resolution electron microscopy. A number of features of woven bone were observed for the first time by these means. Similar to mature crystals from lamellar bone, the apatite crystals in woven bone are also platelet-shaped. However, most likely because of a high rate of old bone resorption and new bone formation in woven material, the average crystal dimensions are considerably smaller than those of mature crystals in lamellar bone. Apatite crystals were noted on the surface of collagen fibrils in woven bone. In densely packed woven bone, the periodicity of mineral deposited on individual fibrils is in registration over many fibrils. In addition to their association with collagen surfaces, crystals also appear distributed in both extrafibrillar and intrafibrillar collagen regions. In both cases, the minerals are crystalline and defect-free. These characteristics provide insight into the spatial and temporal relation between collagen and mineral that is the basis for the structure and organization of the mineral comprising human woven bone.

Apatites↗
PubMed1989

Crystallization of isoelectrically homogeneous cholera toxin.

Past difficulty in growing good crystals of cholera toxin has prevented the study of the crystal structure of this important protein. We have determined that failure of cholera toxin to crystallize well has been due to its heterogeneity. We have now succeeded in overcoming the problem by isolating a single isoelectric variant of this oligomeric protein (one A subunit and five B subunits). Cholera toxin purified by our procedure readily forms large single crystals. The crystal form (space group P2(1), a = 73.0 A, b = 92.2 A, c = 60.6 A, beta = 106.4 degrees, one molecule in the asymmetric unit) has been described previously [Sigler et al. (1977) Science (Washington, D.C.) 197, 1277-1278]. We have recorded data from native crystals of cholera toxin to 3.0-A resolution with our electronic area detectors. With these data, we have found the orientation of a 5-fold symmetry axis within these crystals, perpendicular to the screw dyad of the crystal. We are now determining the crystal structure of cholera toxin by a combination of multiple heavy-atom isomorphous replacement and density modification techniques, making use of rotational 5-fold averaging of the B subunits.

Cholera Toxin↗
PubMed1996

Co-crystallization and characterization of the photosynthetic reaction center-cytochrome c2 complex from Rhodobacter sphaeroides.

The photosynthetic reaction center (RC) of Rhodobacter sphaeroides and cytochrome c2 (cyt c2), its physiological secondary electron donor, have been co-crystallized. The molar ratio of RC/cyt c2 was found by SDS-PAGE and optical absorbance changes in the co-crystals to be 4. The crystals diffracted X-rays to 3.5 angstroms. However, the resolution degraded during data collection. A data set, 82.5% complete, was collected to 4.5 angstroms. The crystals belong to the tetragonal space group P4(3)2(1)2, with unit cell dimensions of a = b = 142.7 angstroms and c = 254.8 angstroms. The positions of the RCs in the unit cell were determined by molecular replacement. A comparable search for the cyt c2 by this method was unsuccessful because of the small contribution of the cytochrome to the total scattering and because of its low occupancy. The cyt c2 was positioned manually into patches of difference electron density, adjacent to the periplasmic surface of the M polypeptide subunit of the RC. The difference electron density was not sufficient for precise positioning of the cyt c2, and its orientation was modeled by placing the exposed edge of the heme toward the primary donor of the reaction center D and by forming pairs for electrostatically interacting RC and cyt c2 amino acid residues. The RC-cyt c2 structure derived from the co-crystal data was supported by use of omit maps and structure refinement analyses. Cyt c2 reduces the photooxidized primary donor D+ in 0.9 +/- 0.1 micros in the co-crystals, which is the same as the fast electron transfer rate in vivo and in solution. This result provides strong evidence that the structure of the complex in the co-crystal is the same as in solution. Two additional methods were used to investigate the structure of the RC-cyt c2 complex: (i) Docking calculations based on interprotein electrostatic interactions identified possible binding positions of the cyt c2 on the RC. The cyt c2 position with the lowest electrostatic energy is very similar to that of the cyt c2 in the proposed co-crystal structure. (ii) Site-directed mutagenesis was used to modify two aspartic acid residues (M184 and L155) on the periplasmic surface of the RC. Cyt c2 binding affinity to these RCs and electron transfer rates to D+ in these RCs support the co-crystal structure of th RC-cyt c2 complex.

Binding Sites↗
PubMed2001

Crystallization, melting, and enzymatic degradation of biodegradable poly(butylene succinate-co-14 mol % ethylene succinate) copolyester.

The crystal structure and growth kinetics of melt-crystallized poly(butylene succinate-co-14 mol % ethylene succinate) [P(BS-co-14 mol % ES)] copolyester have been investigated at a wide crystallization temperature range of 30 to 90 degrees C. By means of wide-angle X-ray diffraction (WAXD), the copolyester composed of BS and ES units has been identified to have the same crystal structure with that of poly(butylene succinate) (PBS) homopolymer, suggesting that only PBS sequences crystallize while that the ES units are in an amorphous form. On the basis of secondary nucleation theory, two regimes of II and III have been observed and their transition temperature is around 80 degrees C. The spherulitic morphologies of P(BS-co-14 mol % ES) copolyester developed from banded spherulites to the normal ones without banding extinction patterns as the crystallization temperature increased. The melting behavior of P(BS-co-14 mol % ES) copolyester under different conditions has been studied by differential scanning calorimetry (DSC). Four melting peaks and one exothermal peak on the melting curves were observed during heating process, and their origination is discussed. The enzymatic degradation was carried out on the melt-crystallized P(BS-co-14 mol % ES) thin film by an extracellar PHB depolymerase from Pseudomonas stutzeri and the morphologies of lamellar crystals before and after degradation have been examined by atomic force microscopy (AFM). The results have indicated that enzymatically degradable ES units exist on the surface of lamellar crystals and are hydrolyzed by the enzyme, while that the crystalline cores composed of PBS chains are not degraded.

Absorbable Implants↗