Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data (633 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
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Paper type: Journal Article,
Impact factor: 2.464, 5-year impact factor: 2.732
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84858964808&partnerID=40&md5=09a3a8a6828305342d630265f6ff2de3
Keywords: Crystal Dehydration, Crystal Quality, Post-Crystallization Treatment, Protein Crystallization, Serum Albumin, X-Ray Crystallography, Apolipoprotein A4, Bovine Serum Albumin, Cytochrome C Oxidase, Dipeptidyl Peptidase, Fatty Acid, Fatty Acid Synthase, Fatty Acid Transporter, Ferredoxin, Ferredoxin Reductase, Glutaryl 7 Aminocephalosporanic Acid Acylase, Hemin, Human Serum Albumin, Lipase Foldase Complex, Local Anesthetic Agent, Maoc Like Dehydratase, Monoclinic Lysozyme, N Acetylglucosamine 1 Phosphate Uridyltransferase, Nectin 1 Ec Complex, Penicillin Amidase, Peptide Deformylase, Phosphoglycerate Kinase, Plasma Protein, Porphobilinogen Synthase, Pyruvate Dehydrogenase, Stat1 Protein, Tetragonal Lysozyme, Thioredoxin, Trehalose Phosphorylase, Tricom Interacting Factor F3, Unclassified Drug, Article, Complex Formation, Crystal Structure, Desiccation, Hanging Drop Vapor Diffusion Method, X Ray Diffraction,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy
Institute of Biostructures and Bioimages, CNR, Via Mezzocannone, 16, Naples I-80134, Italy
Department of Pharmaceutical, Biomedical Sciences, University of Salerno, Via Ponte Don Melillo, I-84084 Fisciano, Italy
References:
Not available.
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.464, 5-year impact factor: 2.732
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84858964808&partnerID=40&md5=09a3a8a6828305342d630265f6ff2de3
Keywords: Crystal Dehydration, Crystal Quality, Post-Crystallization Treatment, Protein Crystallization, Serum Albumin, X-Ray Crystallography, Apolipoprotein A4, Bovine Serum Albumin, Cytochrome C Oxidase, Dipeptidyl Peptidase, Fatty Acid, Fatty Acid Synthase, Fatty Acid Transporter, Ferredoxin, Ferredoxin Reductase, Glutaryl 7 Aminocephalosporanic Acid Acylase, Hemin, Human Serum Albumin, Lipase Foldase Complex, Local Anesthetic Agent, Maoc Like Dehydratase, Monoclinic Lysozyme, N Acetylglucosamine 1 Phosphate Uridyltransferase, Nectin 1 Ec Complex, Penicillin Amidase, Peptide Deformylase, Phosphoglycerate Kinase, Plasma Protein, Porphobilinogen Synthase, Pyruvate Dehydrogenase, Stat1 Protein, Tetragonal Lysozyme, Thioredoxin, Trehalose Phosphorylase, Tricom Interacting Factor F3, Unclassified Drug, Article, Complex Formation, Crystal Structure, Desiccation, Hanging Drop Vapor Diffusion Method, X Ray Diffraction,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cinthia, Naples I-80126, Italy
Institute of Biostructures and Bioimages, CNR, Via Mezzocannone, 16, Naples I-80134, Italy
Department of Pharmaceutical, Biomedical Sciences, University of Salerno, Via Ponte Don Melillo, I-84084 Fisciano, Italy
References:
Not available.
Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data
Serum albumin is one of the most widely studied proteins. It is the most abundant protein in plasma with a typical concentration of 5 g/100 mL and the principal transporter of fatty acids in plasma. While the crystal structures of human serum albumin (HSA) free and in complex with fatty acids, hemin, and local anesthetics have been characterized, no crystallographic models are available on bovine serum albumin (BSA), presumably because of the poor diffraction power of existing hexagonal BSA crystals. Here, the crystallization and diffraction data of a new BSA crystal form, obtained by the hanging drop method using MPEG 5K as precipitating agent, are presented. The crystals belong to space group C2, with unit-cell parameters a = 216.45 A, b = 44.72 A, c = 140.18 A, beta = 114.5°. Dehydration was found to increase the diffraction limit of BSA crystals from ~8 A to 3.2 A, probably by improving the packing of protein molecules in the crystal lattice. These results, together with a survey of more than 60 successful cases of protein crystal dehydration, confirm that it can be a useful procedure to be used in initial screening as a method of improving the diffraction limits of existing crystals.
Serum albumin is one of the most widely studied proteins. It is the most abundant protein in plasma with a typical concentration of 5 g/100 mL and the principal transporter of fatty acids in plasma. While the crystal structures of human serum albumin (HSA) free and in complex with fatty acids, hemin, and local anesthetics have been characterized, no crystallographic models are available on bovine serum albumin (BSA), presumably because of the poor diffraction power of existing hexagonal BSA crystals. Here, the crystallization and diffraction data of a new BSA crystal form, obtained by the hanging drop method using MPEG 5K as precipitating agent, are presented. The crystals belong to space group C2, with unit-cell parameters a = 216.45 A, b = 44.72 A, c = 140.18 A, beta = 114.5°. Dehydration was found to increase the diffraction limit of BSA crystals from ~8 A to 3.2 A, probably by improving the packing of protein molecules in the crystal lattice. These results, together with a survey of more than 60 successful cases of protein crystal dehydration, confirm that it can be a useful procedure to be used in initial screening as a method of improving the diffraction limits of existing crystals.
Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data
Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data
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Impact Factor: 2.208
View Export to BibTeX Export to EndNote
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Impact Factor: 1.76
View Export to BibTeX Export to EndNote
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Impact Factor: 1.76
View Export to BibTeX Export to EndNote
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Impact Factor: 1.283
View Export to BibTeX Export to EndNote
Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
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Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
Impact Factor: 3.067
View Export to BibTeX Export to EndNote
Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
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Impact Factor: 1.492
View Export to BibTeX Export to EndNote
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Impact Factor: 2.244
View Export to BibTeX Export to EndNote
Fogliano V, Monti SM, Ritieni A, Marchisano C, Peluso G, Randazzo G
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Impact Factor: 0.812
View Export to BibTeX Export to EndNote
Cook JA, Kim SY, Teague D, Krishna MC, Pacelli R, Mitchell JB, Vodovotz Y, Nims RW, Christodoulou D, Miles AM, Grisham MB, Wink DA
Convenient colorimetric and fluorometric assays for S-nitrosothiols (590 views)
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Impact Factor: 2.017
View Export to BibTeX Export to EndNote
Marchetti P, Benzi L, Trischitta V, Brunetti A, Cecchetti P, Ciccarone AM, Pezzino V, Vigneri R, Navalesi R
Complementary use of gel permeation and reversed-phase liquid chromatography for the analysis of A14-[125I]insulin and its degradation products in isolated human monocytes (1719 views)
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Impact Factor: 1.588
View Export to BibTeX Export to EndNote
26 Records (26 excluding Abstracts).
Total impact factor: 85.123 (85.123 excluding Abstracts).
Total 5 year impact factor: 100.641 (100.641 excluding Abstracts).
Total impact factor: 85.123 (85.123 excluding Abstracts).
Total 5 year impact factor: 100.641 (100.641 excluding Abstracts).
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