Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data (412 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
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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
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Hunsicker-Wang, L. M., Pacoma, R. L., Chen, Y., Fee, J. A., Stout, C. D., A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus (2005) Acta Crystallogr. D Biol. Crystallogr, 61, pp. 340-343
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Kyrieleis, O. J., Goettig, P., Kiefersauer, R., Huber, R., Brandstetter, H., Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations (2005) J. Mol. Biol, 349, pp. 787-800
Ke, A., Doudna, J. A., Crystallization of RNA and RNA-protein complexes (2004) Methods, 34, pp. 408-414
Bowman, G. D., O'Donnell, M., Kuriyan, J., Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex (2004) Nature, 429, pp. 724-730
Liu, B., Luna, V. M., Chen, Y., Stout, C. D., Fee, J. A., An unexpected outcome of surface engineering an integral membrane protein: Improved crystallization of cytochrome ba (3) from Thermus thermophilus (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 63, pp. 1029-1034
Barton, W. A., Liu, B. P., Tzvetkova, D., Jeffrey, P. D., Fournier, A. E., Sah, D., Cate, R., Nikolov, D. B., Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins (2003) EMBO J, 22, pp. 3291-3302
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Henderson, K. N., Reid, H. H., Borg, N. A., Broughton, S. E., Huyton, T., Anderson, R. P., McCluskey, J., Rossjohn, J., The production and crystallization of the human leukocyte antigen class II molecules HLA-DQ2 and HLA-DQ8 complexed with deamidated gliadin peptides implicated in coeliac disease (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 63, pp. 1021-1025
Callahan, S. J., Morgan, R. D., Jain, R., Townson, S. A., Wilson, G. G., Roberts, R. J., Aggarwal, A. K., Crystallization and preliminary crystallographic analysis of the type IIL restriction enzyme MmeI in complex with DNA (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 67, pp. 1262-1265
Andres, S. N., Junop, M. S., Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 67, pp. 1399-1402
Verma, S. K., Jaiswal, M., Kumar, N., Parikh, A., Nandicoori, V. K., Prakash, B., Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group (2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 65, pp. 435-439
Yap, T. L., Chen, Y. L., Xu, T., Wen, D., Vasudevan, S. G., Lescar, J., A multi-step strategy to obtain crystals of the dengue virus RNA-dependent RNA polymerase that diffract to high resolution (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 63, pp. 78-83
Wheeler, M. J., Russi, S., Bowler, M. G., Bowler, M. W., Measurement of the equilibrium relative humidity for common precipitant concentrations: Facilitating controlled dehydration experiments (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun, 68, pp. 111-114
Matthews, B. W., Solvent content of protein crystals (1968) J. Mol. Biol, 33 (491-497), p. 93
Storoni, L. C., McCoy, A. J., Read, R. J., Likelihood-enhanced fast rotation functions (2004) Acta Crystallogr. D Biol. Crystallogr, 60 (432-438), p. 96
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2012 Mar; 13(3): 3782-3800.
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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
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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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* Biochemical, structural, and computational studies of a γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei (2 views)
Comput Struct Biotechnol J (ISSN: 2001-0370linking), 2022 Jul 27; 20: 4185-4194.
Impact Factor: 6.155
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Scognamiglio PL, Vicidomini C, Fontanella F, De Stefano C, Palumbo R, Roviello GN
* Protein binding of benzofuran derivatives: A CD spectroscopic and in silico comparative study of the effects of 4-nitrophenyl functionalized benzofurans and benzodifurans on BSA protein structure (30 views)
Biomolecules, 2022 Feb; 12: 262-273.
Impact Factor: 6.064
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Caputo T, Cusano AM, Ruvo M, Aliberti A, Cusano A
* Human Serum Albumin Nanoparticles as a Carrier for On-Demand Sorafenib Delivery (14 views)
Curr Pharm Biotechnol (ISSN: 1389-2010linking), 2021 Aug 26; N/D: N/D-N/D.
Impact Factor: 2.097
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Cuocolo A, Pappata S, Zampella E, Assante R
* Advances in SPECT Methodology (273 views)
Int Rev Neurobiol (ISSN: 0074-77429780128154182, 2162-5514electronic), 2018 Sep; 141: 77-96.
Impact Factor: 3.36
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Roviello GN
* Novel insights into nucleoamino acids: biomolecular recognition and aggregation studies of a thymine-conjugated L-phenyl alanine (366 views)
Amino Acids (ISSN: 1438-2199electronic, 0939-4451linking), 2018 May 15; DOI10.1007/s00726-01: 933-941.
Impact Factor: 3.173
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Longo DL, Arena F, Consolino L, Minazzi P, Geninatti-crich S, Giovenzana GB, Aime S
* Gd-AAZTA-MADEC, an improved blood pool agent for DCE-MRI studies on mice on 1 T scanners (393 views)
Biomaterials (ISSN: 0142-9612, 1878-5905electronic, 0142-9612linking), 2015 Oct 16; 75: 47-57.
Impact Factor: 8.387
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Ferraro G, Massai L, Messori L, Merlino A
* Cisplatin binding to human serum albumin: A structural study (413 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2015; 51(46): 9436-9439.
Impact Factor: 6.567
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Romanucci V, Milardi D, Campagna T, Gaglione M, Messere A, D'Urso A, Crisafi E, La Rosa C, Zarrelli A, Balzarini J, Di Fabio G
* Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end (339 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 0968-0896linking), 2014 Feb 1; 22(3): 960-966.
Impact Factor: 2.793
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Caterino M, Merlino A, Balsamo A, Russo Krauss I, Parisi S, Vergara A
* Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy (285 views)
J Solution Chem (ISSN: 0095-9782), 2014 Feb; 43(1): 135-143.
Impact Factor: 1.177
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Ruggiero A, Smaldone G, Squeglia F, Berisio R
* Enhanced crystallizability by protein engineering approaches: A general overview (2032 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2012 Jul; 19(7): 732-742.
Impact Factor: 1.994
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Pilla P, Sandomenico A, Malachovsk V, Borriello A, Giordano M, Cutolo A, Ruvo M, Cusano A
* A protein-based biointerfacing route toward label-free immunoassays with long period gratings in transition mode (374 views)
Biosens Bioelectron (ISSN: 0956-5663, 1873-4235electronic, 0956-5663linking), 2012 Jan 15; 31(1): 486-491.
Impact Factor: 5.437
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Merlino A, Russo Krauss I, Albino A, Pica A, Vergara A, Masullo M, De Vendittis E, Sica F
* Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis (349 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
Impact Factor: 2.598
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Hesse B, Lindhardt TB, Acampa W, Anagnostopoulos C, Ballinger J, Bax JJ, Edenbrandt L, Flotats A, Germano G, Stopar TG, Franken P, Kelion A, Kjaer A, Le Guludec D, Ljungberg M, Maenhout AF, Marcassa C, Marving J, Mckiddie F, Schaefer WM, Stegger L, Underw
* EANM/ESC guidelines for radionuclide imaging of cardiac function (531 views)
Eur J Nucl Med (ISSN: 1619-7070, 1619-7089, 0340-6997), 2008 Apr; 35(4): 851-885.
Impact Factor: 4.532
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Vergara A, Lorber B, Sauter C, Giege R, Zagari A
* Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology (328 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
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Vergara A, Lorber B, Zagari A, Giege R
* Physical aspects of protein crystal growth investigated with the advanced protein crystallization facility in reduced-gravity environments (500 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003; 59(1): 2-15.
Impact Factor: 2.208
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Vergara A, Corvino E, Sorrentino G, Piccolo C, Tortora A, Carotenuto L, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)(10) aboard the International Space Station. 1. Video observation (299 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58: 1690-1694.
Impact Factor: 1.76
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Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (491 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
Impact Factor: 1.76
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (345 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
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Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
Effects of microgravity on the crystal quality of a collagen-like polypeptide (374 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
Impact Factor: 3.067
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Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state (273 views)
J Cryst Growth (ISSN: 0022-0248), 1999; 196(2-4): 305-312.
Impact Factor: 1.492
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Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia CA, Rossi M, Lamzin VS, Wilson KS, Zagari A
Protein crystal growth in the advanced protein crystallization facility on the LMS mission: A comparison of Sulfolobus solfataricus alcohol dehydrogenase crystals grown on the ground and in microgravity (385 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 1998; 54(3): 386-390.
Impact Factor: 2.244
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Fogliano V, Monti SM, Ritieni A, Marchisano C, Peluso G, Randazzo G
An immunological approach to monitor protein lactosylation of heated food model systems (259 views)
Food Chem (ISSN: 0308-8146, 0308-8146print), 1997; 58(1-2): 53-58.
Impact Factor: 0.812
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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 (445 views)
Anal Biochem (ISSN: 0003-2697, 1096-0309electronic, 0003-2697linking), 1996 Jul 1; 238(2): 150-158.
Impact Factor: 2.017
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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 (1706 views)
J Chromatogr B Biomed Sci Appl (ISSN: 0378-4347), 1986 Apr 25; 377(C): 339-344.
Impact Factor: 1.588
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24 Records (24 excluding Abstracts).
Total impact factor: 74.49 (74.49 excluding Abstracts).
Total 5 year impact factor: 94.45 (94.45 excluding Abstracts).
Total impact factor: 74.49 (74.49 excluding Abstracts).
Total 5 year impact factor: 94.45 (94.45 excluding Abstracts).
412 views. Last view on Saturday 24 September 2022, 4:32:01
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