Crystallization and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture

In order to deal with the dynamic ocean environment, blue mussels adhere to various surfacesviatheir collagenous byssal threads. PTMP1 (proximal thread matrix protein 1) is one identified matrix protein residing in the proximal thread and is capable of collagen binding. Its sequence comprises two von Willebrand factor type A-like repeats. In order to characterize the structure and domain architecture of PTMP1, recombinant protein was crystallized by vapour diffusion. The obtained crystals diffracted to 1.95 Å resolution and belonged to space groupP21, with unit-cell parametersa= 62.0,b= 62.3,c= 122.6 Å, β = 102.2°. The Matthews coefficient suggested the presence of two monomers in the asymmetric unit and 48.3% solvent content.

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Crystallization and preliminary X-ray diffraction analysis of Xyn30D fromPaenibacillus barcinonensis

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x14012035 ◽

2014 ◽

Vol 70 (7) ◽

pp. 963-966 ◽

Cited By ~ 2

Author(s):

María Ángela Sainz-Polo ◽

Susana Valeria Valenzuela ◽

F. Javier Pastor ◽

Julia Sanz-Aparicio

Keyword(s):

Catalytic Domain ◽

Domain Architecture ◽

Glycoside Hydrolase Family ◽

Carbohydrate Binding ◽

X Ray Diffraction ◽

Full Data ◽

Data Set ◽

X Ray ◽

Hydrolysis Of ◽

Hydrolase Family

Xyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N-terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C-terminal family 35 carbohydrate-binding domain (CBM35) able to bind xylans and glucuronic acid. Xyn30D shares the characteristic endo mode of action described for GH30 xylanases, with the hydrolysis of the β-(1,4) bonds of xylan being directed by α-1,2-linked glucuronate moieties, which have to be placed at the −2 subsite of the xylanase active site. Crystals of the complete enzyme were obtained and a full data set to 2.3 Å resolution was collected using a synchrotron X-ray source. This represents the first bimodular enzyme with the domain architecture GH30-CBM35. This study will contribute to the understanding of the role that the different xylanases play in the depolymerization of glucuronoxylan.

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Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains

FEBS Letters ◽

10.1016/0014-5793(96)00133-0 ◽

1996 ◽

Vol 382 (1-2) ◽

pp. 15-17 ◽

Cited By ~ 16

Author(s):

Antonio Romero ◽

Paloma F Varela ◽

Libia Sanz ◽

Edda Töpfer-Petersen ◽

Juan J Calvete

Keyword(s):

Diffraction Analysis ◽

Seminal Plasma ◽

X Ray Diffraction ◽

X Ray

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Crystallization and preliminary X-ray diffraction analysis of bovine seminal plasma PDC-109, a protein composed of two fibronectin type II domains

Proteins Structure Function and Bioinformatics ◽

10.1002/(sici)1097-0134(199707)28:3<454::aid-prot14>3.0.co;2-g ◽

1997 ◽

Vol 28 (3) ◽

pp. 454-456 ◽

Cited By ~ 11

Author(s):

Antonio Romero ◽

Paloma F. Varela ◽

Edda Töpfer-Petersen ◽

Juan J. Calvete

Keyword(s):

Diffraction Analysis ◽

Seminal Plasma ◽

Type Ii ◽

X Ray Diffraction ◽

X Ray ◽

Fibronectin Type

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The Use of Advanced Analytical Techniques for Characterization of the Chemical, Physical, and Crystallographic Nature of a Surface

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100071107 ◽

1973 ◽

Vol 31 ◽

pp. 132-133 ◽

Cited By ~ 1

Author(s):

R. E. Herfert

Keyword(s):

Surface Characterization ◽

Analytical Techniques ◽

X Ray Diffraction ◽

Depth Of Penetration ◽

X Ray ◽

The Past ◽

Transmission Electron ◽

Scanning Electron

Studies of the nature of a surface, either metallic or nonmetallic, in the past, have been limited to the instrumentation available for these measurements. In the past, optical microscopy, replica transmission electron microscopy, electron or X-ray diffraction and optical or X-ray spectroscopy have provided the means of surface characterization. Actually, some of these techniques are not purely surface; the depth of penetration may be a few thousands of an inch. Within the last five years, instrumentation has been made available which now makes it practical for use to study the outer few 100A of layers and characterize it completely from a chemical, physical, and crystallographic standpoint. The scanning electron microscope (SEM) provides a means of viewing the surface of a material in situ to magnifications as high as 250,000X.

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Ribosome Structural Organization

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100051670 ◽

1974 ◽

Vol 32 ◽

pp. 332-333

Author(s):

James A. Lake

Keyword(s):

Ribosomal Proteins ◽

Structural Organization ◽

Three Dimensional ◽

Small Subunit ◽

Structural Studies ◽

X Ray Diffraction ◽

Specific Antibodies ◽

X Ray ◽

E Coli ◽

Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

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Electron Microscopy of Human Gallstones

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065523 ◽

1971 ◽

Vol 29 ◽

pp. 296-297

Author(s):

C. Wolpers ◽

R. Blaschke

Keyword(s):

Electron Microscopy ◽

Room Temperature ◽

Bile Pigment ◽

X Ray Diffraction ◽

Triclinic Crystal System ◽

X Ray ◽

Follow Up Study ◽

Infra Red ◽

Main Components

Scanning microscopy was used to study the surface of human gallstones and the surface of fractures. The specimens were obtained by operation, washed with water, dried at room temperature and shadowcasted with carbon and aluminum. Most of the specimens belong to patients from a series of X-ray follow-up study, examined during the last twenty years. So it was possible to evaluate approximately the age of these gallstones and to get information on the intensity of growing and solving.Cholesterol, a group of bile pigment substances and different salts of calcium, are the main components of human gallstones. By X-ray diffraction technique, infra-red spectroscopy and by chemical analysis it was demonstrated that all three components can be found in any gallstone. In the presence of water cholesterol crystallizes in pane-like plates of the triclinic crystal system.

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High Resolution Replication of Organoclay Surfaces

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100055126 ◽

1982 ◽

Vol 40 ◽

pp. 576-577

Author(s):

W. W. Barker ◽

W. E. Rigsby ◽

V. J. Hurst ◽

W. J. Humphreys

Keyword(s):

Clay Mineral ◽

Organic Molecule ◽

Organic Molecules ◽

X Ray Diffraction ◽

Xrd Pattern ◽

X Ray ◽

Naturally Occurring ◽

Silicate Layers ◽

Mineral Identification

Experimental clay mineral-organic molecule complexes long have been known and some of them have been extensively studied by X-ray diffraction methods. The organic molecules are adsorbed onto the surfaces of the clay minerals, or intercalated between the silicate layers. Natural organo-clays also are widely recognized but generally have not been well characterized. Widely used techniques for clay mineral identification involve treatment of the sample with H2 O2 or other oxidant to destroy any associated organics. This generally simplifies and intensifies the XRD pattern of the clay residue, but helps little with the characterization of the original organoclay. Adequate techniques for the direct observation of synthetic and naturally occurring organoclays are yet to be developed.

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