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Biophys J. 1997 March; 72(3): 1425–1433. | PMCID: PMC1184525 |
Modification of calcite crystal growth by abalone shell proteins: an atomic force microscope study. D A Walters, B L Smith, A M Belcher, G T Paloczi, G D Stucky, D E Morse, and P K Hansma Department of Physics, University of California, Santa Barbara 93106, USA. deronwal@physics.ucsb.edu Abstract A family of soluble proteins from the shell of Haliotis rufescens was introduced over a growing calcite crystal being scanned in situ by an atomic force microscope (AFM). Atomic step edges on the crystal surface were altered in shape and speed of growth by the proteins. Proteins attached nonuniformly to the surface, indicating different interactions with crystallographically different step edges. The observed changes were consistent with the habit modification induced by this family of proteins, as previously observed by optical microscopy. To facilitate further studies in this area, AFM techniques and certain AFM imaging artifacts are discussed in detail. Full text Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (3.8M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References. Images in this article Click on the image to see a larger version. These references are in PubMed. This may not be the complete list of references from this article. - Berman Amir, Hanson Jonathan, Leiserowitz Leslie, Koetzle Thomas F, Weiner Stephen, Addadi Lia. Biological Control of Crystal Texture: A Widespread Strategy for Adapting Crystal Properties to Function. Science. 1993 Feb 5;259(5096):776–779. [PubMed]
- Cleveland JP, Schäffer TE, Hansma PK. Probing oscillatory hydration potentials using thermal-mechanical noise in an atomic-force microscope. Phys Rev B Condens Matter. 1995 Sep 15;52(12):R8692–R8695. [PubMed]
- Dussol B, Geider S, Lilova A, Léonetti F, Dupuy P, Daudon M, Berland Y, Dagorn JC, Verdier JM. Analysis of the soluble organic matrix of five morphologically different kidney stones. Evidence for a specific role of albumin in the constitution of the stone protein matrix. Urol Res. 1995;23(1):45–51. [PubMed]
- Hansma HG, Laney DE, Bezanilla M, Sinsheimer RL, Hansma PK. Applications for atomic force microscopy of DNA. Biophys J. 1995 May;68(5):1672–1677. [PubMed]
- Land TA, Malkin AJ, Kuznetsov YG, McPherson A, De Yoreo JJ Mechanisms of protein crystal growth: An atomic force microscopy study of canavalin crystallization. Phys Rev Lett. 1995 Oct 2;75(14):2774–2777. [PubMed]
- Malkin AJ, Kuznetsov YuG, Land TA, DeYoreo JJ, McPherson A. Mechanisms of growth for protein and virus crystals. Nat Struct Biol. 1995 Nov;2(11):956–959. [PubMed]
- Thomson NH, Fritz M, Radmacher M, Cleveland JP, Schmidt CF, Hansma PK. Protein tracking and detection of protein motion using atomic force microscopy. Biophys J. 1996 May;70(5):2421–2431. [PubMed]
- Walsh Dominic, Hopwood Jeremy D, Mann Stephen. Crystal Tectonics: Construction of Reticulated Calcium Phosphate Frameworks in Bicontinuous Reverse Microemulsions. Science. 1994 Jun 10;264(5165):1576–1578. [PubMed]
- Wierzbicki A, Sikes CS, Madura JD, Drake B. Atomic force microscopy and molecular modeling of protein and peptide binding to calcite. Calcif Tissue Int. 1994 Feb;54(2):133–141. [PubMed]
- Worcester EM. Urinary calcium oxalate crystal growth inhibitors. J Am Soc Nephrol. 1994 Nov;5(5 Suppl 1):S46–S53. [PubMed]
- Yip CM, Ward MD. Atomic force microscopy of insulin single crystals: direct visualization of molecules and crystal growth. Biophys J. 1996 Aug;71(2):1071–1078. [PubMed]
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